Nucleoside triphosphate-binding proteins: Different scaffolds to achieve phosphoryl transfer

Quarterly Reviews of Biophysics

Volumn 32, Issue 1, 1999, Pages 1-56

  Vetter, Ingrid R ^a   Wittinghofer, Alfred ^a  

^a TU DORTMUND UNIVERSITY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

6 PHOSPHOFRUCTOKINASE; ABC TRANSPORTER; ADENYLATE CYCLASE; APYRASE; CHAPERONE; CREATINE KINASE; DNA TOPOISOMERASE (ATP HYDROLYSING); GLUTAMATE AMMONIA LIGASE; GUANINE NUCLEOTIDE BINDING PROTEIN; LUCIFERASE; NUCLEOSIDE TRIPHOSPHATE; PHOSPHOGLYCERATE KINASE; POLYDEOXYRIBONUCLEOTIDE SYNTHASE; PROTEIN KINASE; PYRUVATE KINASE; RAS PROTEIN;

DEPHOSPHORYLATION; ENZYME SUBSTRATE COMPLEX; HUMAN; NONHUMAN; PRIORITY JOURNAL; REVIEW; STRUCTURE ACTIVITY RELATION;

ADENINE NUCLEOTIDES; ANIMALS; CARRIER PROTEINS; HUMANS; HYDROLASES; MODELS, MOLECULAR; NUCLEOTIDES; PHOSPHOTRANSFERASES; PROTEIN CONFORMATION;

EID: 0033511228     PISSN: 00335835     EISSN: None     Source Type: Journal    
DOI: 10.1017/S0033583599003480     Document Type: Review

References (344)

1. 5A, showing the pathway of phosphoryl transfer. Protein Science 4, 1262-1271.
2. ABERG, A., YAREMCHUK, A., TUKALO, M., RASMUSSEN, B. & CUSACK, S. (1997). Crystal structure analysis of the activation of histidine by Thermus thermophilus histidyl-tRNA synthetase. Biochemistry 36, 3084 3094.
3. 1-ATPase from bovine heart mitochondria. Nature 370, 621-628.
4. ADAMS, J. A. & TAYLOR, S. S. (1992). Energetic limits of phosphotransfer in the catalytic subunit of cAMP-dependent protein kinase as measured by viscosity experiments. Biochemistry 31, 8516-8522.
5. ADMIRAAL, S. & HERSCHLAG, D. (1995). Mapping the transition state for ATP hydrolysis: implications for enzymatic catalysis. Chemistry & Biology 2, 729 739.
6. AHMADIAN, M. R., MITTAL, R., HALL, A., & WITTINGHOFER, A. (1997). Aluminum flouride associates with the small guanine nucleotide binding proteins. FEBS Lett. 408, 315-318.
7. AL-KARADAGHI, S., AEVARSSON, A., GARBER, M., ZHELTONOSOVA, J. & LILJAS, A. (1996). The structure of elongation factor G in complex with GDP conformational flexibility and nucleotide exchange. Structure 4, 555-565.
8. ALMASSY, R. J., JANSON, C. A., HAMLIN, R., XUONG, N. H. & EISENBERG, D. (1986). Novel subunit-subunit interactions in the structure of glutamine synthetase. Nature 323, 304-309.
9. ANDERSON, C. M., STENKAMP, R. E., STEITZ, T. A. (1978). Sequencing a protein by X-ray crystallograpby, 11. Refinement of yeast hexokinase B coordinates and sequence at 2.1 ängstroms resolution. J. Mol. Biol. 123, 15-33.
10. ANDERSON, C. M., ZUCKER, E. H. & STEITZ, T. A. (1979). Space-filling models of kinase clefts and conformation changes. Science 204, 375-380.
11. ARAVIND, L, GALPERIN, M. Y. & KOONIN, E. V. (1998). The catalytic domain of the P-typE ATPases has the haloacid dehalogenase fold. TIBS 23, 127 129.
12. ARNEZ, J. G. & MORAS, D. (1997). Structural and functional considerations of the aminoacylation reaction. TrendS Biochem. Sci. 22, 189-232.
13. ARNEZ, J. G., HARRIS, D. C., MITSCHLER, A., REES, B., FRANCKLYN, C. S. & MORAS, D. (1995). Crystal structure of histidyl-tRNA synthetase from E. coli complexed with histidyl-adenylate. EMBO J. 14, 4143-4155.
14. ARNEZ, J. G., AUGUSTINE, J. G. MORAS, D. & FRANCKLYN, C. S. (1997). The first step of amino-acylation at the atomic level in histidyl-tRNA synthetase. Proc. Natl. Acad. Sci. USA 94, 7144-7149.
15. ARNOLD, E., JACOBO-MOLINA, A., NANNI, R. G., WILLIAMS, R. L., LU, X., DING, J., CLARK JR., A. D., ZHANG, A., FERRIS, A. L., CLARK, P., HIZI, M. & HUGHES, S. H. (1992). Structure of HIV-1 reverse transcriptase/DNA complex at 7 Å resolution showing active site locations. Nature 357, 85-89.
16. ARTYMIUK, P. J., GRINDLEY, H. M., KUMAR, K., RICE, D. W. & WILLET, P. (1993).Three-dimensional structural resemblance between the ribonuclease H and connection domains of HIV reverse transcriptase and the ATPase fold revealed by graph theoretical techniques, FEBS 324, 15-21.
17. ARTYMIUK, P. J., POIRRETTE, A. R., RICE, D. W. & WILLETT, P. (1996). Biotin carboxylase comes into fold. Nature Struct. Biol. 3, 128 132.
18. + ATPase in the open conformation. Nature 392, 840-843.
19. AUERBACH, G., HUBER, R. GRÄTTINGER, M., ZAISS, K., SCHURIG, H., JAENICKE, R. & JACOB, U. (1997). Closed structure of phosphoglycerate kinase from Thermotoga maritima reveals the catalytic mechanism and determinants of thermal stability. Structure 5, 1475 1483.
20. AUSTIN, S., KUNDROT, C. & DIXON, R. (1991). Influence of a mutation in the putative nucleotide binding site of the nitrogen regulatory protein NTRC on its positive control function. Nucleic Acids Res. 19, 2281-2287.
21. AUZAT, I., LE BRAS, G. & GAREL, J.-R. (1994). The cooperativity and allosteric inhibition of Escberichia coli phosphofructokinase depend on the interaction between threonine-125 and ATP. Proc. Natl. Acad. Sci. USA 91, 5242-5246.
22. BAEK, Y. H. & NOWAK, T. (1982). Kinetic evidence for a dual cation role for muscle pyruvate kinase. Arch. Biochem. Biophys. 217, 491-497.
23. BAIROCH, A., BUCHNER, P. & HOFMANN, K. (1997). The PROSITE, database, its status in 1997. Nucl. Acids Res. 25, 217-221.
24. BALDWIN, T. O. (1996). Firefly luciferase: the structure is known, but the mystery remains. Structure 15, 223-228.
25. BALDWIN, T. O. CHRISTOPHER, J. A., RAUSHEL, F. M., SINCLAIR, J. F., ZIEGLER, M. M., FISHER, A. J. & RAYMENT, I. (1995). Structure of bacterial luciferase. Curr. Op. in Struc. Biology 5, 798-809.
26. BARNES, L. D., GARRISON, P. N., SIPRASHVILI, Z., GURANOWSKI, A., ROBINSON, A. K., INGRAM, S. W., CROCE, C. M., OHTA, M. & HUEBNER, K. (1996). Fhit, a putative tumor suppressor in humans, is a dinucleoside 5′,5′"-P1 ,P3-triphosphate hydrolase. Biochemistry 35, 11529-11535.
27. BASS, M. B., FROMM, H. J. & RUDOLPH, F. B. (1984). The mechanism of the adenylosuccinate synthetase reaction as studied by positional isotope exchange. J. biol. Chem. 259, 12330-12333.
28. BATES, A. D., O'DEA, M. H., & GELLERT, M. (1996). Energy coupling in E. coli DNA gyrase: the reationship between nucleotide binding, strand passage, and DNA supercoiling. Biochemistry 35, 1408-1416.
29. BELRHALI, H., YAREMCHUK, A.D., TUKALO, M. A., LARSEN, K., BERTHET-COLOMINAS, C., LEBERMAN, R., BEIJER, B., SPROAT, B., ALS-NIELSEN, J., GRUBEL, G., LEGRAND, J.-F., LEHMANN, M. & CUSACK, S. (1994). Crystal structures of 2.5 Å resolution of seryl-tRNA synthetase complexed with two different analogues of seryl-adenylate. Science 263, 1432-1436.
30. p4A synthesis bv seryl-tRNA synthetase. Structure 3, 341-352.
31. BENEDETTI, P., SILVESTRI, A., FIORANI, P. & WANG, J. C. (1997). Study of yeast DNA topoisomerase and its truncation derivatives by transmission electron microscopy. J. Biol. Chem. 272, 12132-12137.
32. BENNETT JR, W. S. & STEITZ, T. A. (1980). Structure of a complex between yeast hexokinase A and glucose. I. Structure determination and refinement at 3.5 Ångstroms resolution. J. Mol. Biol. 140, 183-209.
33. BERCHTOLD, H., RESHETNIKOVA, L., REISER, C. P. A., SCHIRMER, N. K., SPRINZL, M. & HILGENFELD, R. (1993). Crystal structure of active elongation factor Tu reveals major domain rearrangements. Nature 365, 126-132.
34. BERNSTEIN, B. E., MICHELS, P. A. M. & HOL, W. G. J. (1997). Synergistic effects of the substrate-induced conformational changes in phosphoglycerate kinase activation. Nature 385, 275-278.
35. BERTHET-CoLOMINAS, C., SEIGNOVERT, L., HARTLEIN, M., GROTLI, M., CUSACK, S. & LEBERMAN, R. (1998). The crystal structure of asparaginyl-tRNA syntetase from Thermus thermophilus and its complexes with ATP and asparaginyl-adenylate - the mechanism of discrimination between asparagine and aspartic acid. EMBO J. 17, 2947-2960.
36. BERGER, J. M. (1998). Type II DNA topoisomerases. Curr. Op. Struc. biol. 8, 26-32.
37. BERGER, J. M., GAMBLIN, S. J., HARRISON, S. C. & WANG, J. C. (1996). Structure and mechanism of DNA topoisomerase II. Nature 379, 225-232.
38. BESSMAN, M. J., FRICK, D. N. & O'HANDLEY, S. F. (1996). The MutT proteins or 'nudix' hydrolases, a family of versatile, widely distributed, 'housecleaning' enzymes. J. biol. Chem. 271, 25059-25062.
39. BIRD, L. E., HOSAHALLI, S., SUBRAMANYA, S. & WIGLEY, D. B. (1998). Helicases: a unifying structural theme? Curr. Op. Struct. Biol. 8, 14-18 .
40. BLAKE, C. C. & EVANS, P. R. (1974). Structure of horse muscle phosphoglycerate kinase, some results on the chain conformation, substrate binding and the evolution of the molecule from a 3 Ångstroms fourier map. J. Mol. Biol. 84, 585-601.
41. BLOCK, S. M. (1997). Real engines of creation. Nature 386, 217-219
42. BOISVERT, D. C., WANG, J., OTWINOWSKI, Z. HORWICH, A. L. & SIGLER, P. B. (1996). The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATPγS. Nature Struct. biol. 3, 170-177.
43. BORK, P. & KOONIN, E. V. (1994). A P-loop-like motif in a widespread ATP pyrophosphatase domain: Implications for the evolution of sequence motifs and enzyme activity. Proteins 20, 347-355.
44. BORK, P., SANDER, C. & VALENCIA, A. (1992). An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins. Proc. Natl. Acad. Sci. 89, 7290-7294.
45. BORK, P., HOLM, L., KOONIN, E. & SANDER, C. (1995). The cytidylyltransferase superfamily : identification of the nucleotide binding site and fold prediction. Proteins 22, 259-266.
46. 2+ adenylyl imidodiphosphate and inhibitor peptide PKI(5-24). EMBO J. 12, 849-859.
47. BRAIG, K., OTWINOWSKI, Z., HEGDE, R., BOISVERT, D. C., JOACHIMIAK, A., HORWICH, A. L. & SIGLER, P. B. (1994). The crystal structure of the bacterial chaperonin GroEL at 2.8 Å. Nature 371, 578-586.
48. BRANDEN, C. & TOOZE, J. (1991). In introduction to Protein Structure. Garland Publishing, Inc. N. Y. and London 1991 p.134
49. BRAUTIGAM, C. A. & STEITZ, T. A. (1998). Structural and functional insights provided by crystal structures of DNA polymerases and their substrate complexes. Curr. Op. Struc. Biol. 8, 54-63.
50. BRENNER, C., GARRISON, P., GILMOUR, J., PEISACH, D., RINGE, D., PETSKO, G. A. & LOWENSTEIN, J. M. (1997). Crystal structures of HINT demonstrate that histidine triad proteins are GalT-related nucleotide-binding proteins. Nat. Struc. Biol. 4, 231-238.
51. BRICK, P., BHAT, T. N. & BLOW, D. M. (1989). Structure of tyrosyl transfer RNA synthetase refined at 2-3 Å resolution interaction of the enzyme with the tyrosyl adenylate intermediate. J. Mol. Biol. 208, 83-98.
52. BROWN, D. G., VISSE, R., SANDHU, G., DAVIES, A., RIZKALLAH, P. J., MULITZ, C., SUMMERS, W. C. & SANDERON, M. R. (1995). Crystal structure of the thymidine kinase from herpes simplex virus type-I in complex with deoxythymidine and ganciclovir. Nature Struct. Biol. 2, 876-881.
53. BRUNIE, S., ZELWER, C. & RISLER, J. L. (1990). Crystallographic study at 2.5 Å resolution of the interaction of methionyl transfer RNA synthetase from Escherichia coli with ATP. J. Mol. Biol. 216, 411-424.
54. BRYANT, T. N., WATSON, H. C. & WENDELL, P. L. (1974). Structure of yeast phosphoglycerate kinase. Nature 247, 14-17.
55. BRYANT, S. H., MADEJ, T., JANIN, J., LIU, Y., RUOHO, A. E., ZHANG, G. & HURLEY, J. H. (1997). reply to previous letter. Nature 388, 34-34.
56. BUKAU, B. & HORWICH, A. L. (1998). The Hsp70 and Hsp60 chaperone machines. Cell 92, 351-366.
57. CABRAL, J. H., JACKSON, A. P., SMITH, C. V., SHIKOTRA, N., MAXWELL, A. & LIDDINGTON, R. C. (1997). Crystal structure of the breakage-reunion domain of DNA gyrase. Nature 388, 903-906.
58. CANANGARAJAH, B. J., KHOKHLATCHEV, A., COBB, M. H. & GOLDSMITH, E. J. (1997). Activation mechanism of the MAP kinase ERK2 by dual phosphorylation. Cell 90, 859-869.
59. CAVARELLI, J., ERIANI, G., REES, B., RUFF, M., BOEGLIN, M., MITSCHLER, A., MARTIN, F., GANGLOFF, J., THIERRY, J.-C. & MORAS, D. (1994). The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation reaction. EMBO J. 13, 327-337.
60. CEDERGREN-ZFPPEZAUER, E. S., LARSSON, G., NYMAN, P. O., DAUTER, Z. & WILSON, K. S. (1992). Crystal structure of a dUTPase. Nature 355, 740-743.
61. CHAMPOUX, J. J. (1990). In DNA Topology and its Biological Effects. Cold Spring Harbour NY: Cold Spring Harbour Lab., pp. 217-242.
62. CHEN, S., ROSEMAN, A. M., HUNTER, A. S., WOOD, S. P., BURSTON, S. G., RANSON, N. A., CLARKE, A. R. & SAIBIL, H. R. (1994). Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy. Nature 37, 261-264.
63. CHIN, D. T., GOFF, S. A., WEBSTER, T., SMITH, T. & GOLDBERG, A. L. (1988). Sequence of the Ion gene in Escherichia coli. A heat-shock gene which encodes the ATP-dependent protease La. J. Biol. Chem. 263, 11718-11728.
64. CLEVES, A. E. & KELLY, R. B. (1996). Protein translocation: rehearsing the ABCs. Current Biology 6, 276-278.
65. COHN, M. (1959). Mechanisms of enzymatic cleavage of some organic phosphates. J. Cell. Comp. Physiol. 54, Suppl. 1, 17-31.
66. COLEMAN, D. E., BERGHUIS, A. M., LEE, E., LINDER, M. E., GILMAN, A. G. & SPRANG, S. R. (1994). Structures of active conformations of Gial and the mechanism of GTP hydrolysis. Science 265, 1405-1412.
67. CONTI, E., FRANKS, N. P. & BRICK, P. (1996). Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes. Structure 4, 287-298.
68. CUSACK, S. (1995). Eleven down and nine to go. Nat. Struct. Biol. 2, 824-831.
69. CUSACK, S. (1997). Aminoacyl-tRNA synthetases. Curr. Opinion Struct. Biol. 7, 881 -889.
70. CUSACK, S., BERTHET-COLOMINAS, C., HÄRTLRIN, M., NASSAR, N. & LEBERMAN, E. (1990). A second class of synthetase structure revealed by X-ray analysis of E. coli seryl-tRNA synthetase at 2.5 Å resolution. Nature 347, 249-255.
71. CUSACK, S., YAREMCHUK, A., KRIKLIVIY, I. & TUKALO, M. (1998). tRNA(Pro) anticodon recognition by Thermus thermophilus prolyl-tRNA synthetase. Structure 6, 101-108.
72. DAVIES, G. J., GAMBLIN, S. J., LITTLECHILD, J. A., DAUTER, Z. & WATSON, H. C. (1994). Structure of the ADP complex of the 3-phosphoglycerate kinase from Bacillus stearothermophilus at 1.65 Ångstroms. Acta Cryst. D50, 202-209.
73. DAVIES II, J. F., ALMASSY, R. J., HOSTOMSKA, Z., FERRE, R. A. & HOSTOMSKY, Z. (1994). 2.3 Ångstroms crystal structure of the catalytic domain of DNA polymerase β Cell 76, 1123-1133.
74. DEBONDT, H. L., ROSENBLATT, J., JANCARIK, J., JONES, H. D., MORGAN, D. O. & KIM, S.-H. (1993). Crystal structure of cyclin-dependent kinase 2. Nature 363, 595-602.
75. DELARUE, M., POCH, O., TORDO, N., MORAS, D. & ARGOS, P. (1990). An attempt to unify the structure of polymerases. Protein Eng. 3, 461-467.
76. DELARUE, M., POTERSZMAN, A., NIKONOV, S., GARBER, M., MORAS, D. & THIERRY, J. C. (1994). Crystal structure of a prokaryotic aspartyl tRNA-synthetase. EMBO J. 13, 3219-3229.
77. DITZEL, L., LOWE, J., STOCK, D., STETTER, K. O., HUBER, H., HUBER, R. & STEINBACHER, S. (1998). Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT. Cell 93, 125-138.
78. DREUSICKE, D., KARPLUS, P. A. & SCHULZ, G. E. (1988). Refined structure of porcine cytosolic adenylate kinase at 2.1 Å resolution. J. Mol. Biol. 199, 359-371.
79. DOUBLIÉ, S., BRICOGNE, G., GILMORE, C. & CARTER, C. W. JR. (1995). Tryptophanyl-tRNA synthetase crystal structure reveals an unexpected homology to tyrosyl-tRNA synthetase. Structure 3, 17-31.
80. DOUBLIÉ, S., TABOR, S., LONG, A. M., RICHARDSON, C. C. & ELLENBERGER, T. (1998). Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution. Nature 391, 251-258.
81. DRUCK, T., HADACZEK, P., FU, T. B., OHTA, M., SIPRASHVILI, Z., BAFFA, R., NEGRINI, M., KASTURY, K., VERONESE, M. L., ROSEN, D., ROTHSTEIN, J., MCCuE, P., COTTICELLI, M. G., INOUE, H., CROCE, C. M. & HUEBNER, K. (1997). Structure and expression of the human FHIT gene in normal and tumor cells. Cancer Res. 57, 504-512.
82. DUMAS, C., LASCU, I., MORERA, S., GLASER, P. FOURME, R., WALLET, V., LACOMBE, M.-L., VERON, M. & JANIN, J. (1992). X-ray structure of nucleoside diphosphate kinase. EMBO J. 11, 3203-3208.
83. EGELMAN, E. H. (1996). Homomorphous hexameric helicases. Tales from the ring cycle. Structure 4, 759-762.
84. EOM, S. H., WANG, J. & STEITZ, T. A. (1996). Structure of Taq polymerase with DNA at the polymerase active site. Nature 382, 278-281.
85. ERIANIE, G., DELARUE, M., POCH, O., GANGLOFF. J. & MORAS, D. (1990). Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature 347, 203-206.
86. ESSER, L., WANG, C.-R., HOSAKA, M., SMAGULA, S., SÜDHOF, T. C. & DEISENHOFER, J. (1998). Synapsin I is structurally similar to ATP-utilizing enzymes. EMBO J 17, 77-84.
87. EVANS, P. R., FARRANTS, G. W. & HUDSON, P. J. (1981). Phosphofructokinase. Structure and control. Phil. Trans. R. Soc. London 293, 53-62.
88. FAN, C., MOEWS, P. C., WALSH, C. T. & KNOX, J. R. (1994). Vancomycin resistance: Structure of D-Alanine: D-Alanine ligase at 2.3 Ångstroms. Science 266, 439-443.
89. FAN, C., MOEWS, P. C., SHI, Y., WALSH, C. T. & KNOX, J. R. (1995). A common fold for peptide synthetases cleaving ATP to ADP: glutathione synthetase and D-alanine: d-alanine ligase of Escherichia coli. Proc. Natl. Acad. Sci USA 92, 1172-1176.
90. +-ATPase: a universal proton pump of eukaryotes. Biochem. J. 324, 697-712.
91. 4. Biochemistry 34, 8960-8972.
92. FLAHERTY, K. M., DELUCA-FLAHERTY, C. R. & MCKAY, D. B. (1990). Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein. Nature 346, 623-628.
93. FREYMANN, D. M., KEENAN, R. J., STROUD, R. M. & WALTER, P. (1997). Structure of the conserved GTPase domain of the signal recognition particle. Nature 385, 361-364.
94. FRICK, D. N., WEBER, D. J., ABEYGUNAWARDANA, A., GITTIS, A. G., BESSMAN, M. J. & MILDVAN, A. S. (1995). NMR Studies of the conformations and location of nucleotides bound to the Escherichia coli MutT enzyme. Biochemistry 34, 5577-5586.
95. FRITZ-WOLF, K., SCHNYDER, T., WALLIMANN, T. & KABSCH, W. (1996). Structure of mitochondrial creatine kinase. Nature 381, 341-345.
96. GALPERIN, M. Y. & KOONIN, E. V. (1997). A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity. Protein Science 6, 2639-2643.
97. GEORGIADIS, M. M., KOMIYA, H., CHAKRABARTI, P., Woo, D., KORNUC, J. J. & REES, D. C. (1992). Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii. Science 257, 1653-1659.
98. GEORGIADIS, M. M., JESSEN, S. M., OGATA, C. M., TELESNITSKY, A., GOFF, S. P. & HENDRICKSON, W. A. (1995). Mechanistic implications from the structure of a catalytic fragment of Moloney murine leukaemia virus reverse transcriptase. Structure 3, 879-892.
99. GERMANN, U. A., PASTAN, I. & GOTTESMAN, M. M. (1996). P-glycoproteins: mediators of multidrug resistance. Sem. Cell biol. 4, 63-76.
100. GERSTEIN, M. (1997). A structural census of genomes: comparing bacterial, eucaryotic, and archaeal genomes in terms of protein structure. J. Mol. Biol. 274, 562-576.
101. GOLDBERG, J., NAIRN, A. C. & KURIYAN, J. (1996). Structural basis for the autoinhibition of calcium/calmodulin-dependent protein Kinase I. Cell 84, 875 -887.
102. phe. Structure 5, 59-68.
103. GORBALENYA, A. E. & KOONIN, E. V. (1990). Superfamily of UvrA-related NTP-binding proteins. Implications for rational classification of recombination/repair systems. J. Mol. Biol. 213, 583-591.
104. GOTTESMAN, J., SQUIRES, C., PICHERSKY, E., CARRINGTON, M., HOBBS, M., MATTICK, J. S., DALRYMPLE:, B., KURAMITSU, H., SHIROZY, T., FOSTER, T. et al. (1990). Conservation of the Regulatory Subunit for the Clp ATP-dependent Protease in Prokaryotes and Eukaryotes. Proc. Natl. Acad. Sci. USA 87, 3513-3517.
105. GREENSPAN, D. L., CONNOLLY, D. C., WU, R., LEI, R. Y., VOGELSTEIN, J. T. C., KIM, Y. T., MOK, J. E., MUNOZ, N., BOSCH, F. X., SHAH, K. & CHO, K. R. (1997). Loss of FHIT expression in cervical carcinoma cell lines and primary tumors. Cancer Research 57, 4692-4698.
106. GUPTA, R. K., OESTERLING, R. M. & MILDVAN, A. S. (1976). Dual divalent cation requirement for activation of pyruvate kinase: essential roles of both enzyme- and nucleotide-bound metal ion. Biochemistry 15, 2881-2887.
107. HÅKANSSON, K., DOHERTY, A. J., SHUMAN, S. & WIGLEY, D. B. (1997). X-ray crystallography reveals a large conformational change during guanyl transfer by mRNA capping enzymes. Cell 89, 545-553.
108. HANKS, S. K., QUINN, A. M. & HUNTER, T. (1988). The protein kinase family : conserved features and deduced phylogeny of the catalytin domains. Science 241, 42-52.
109. HANKS, S. K. & HUNTER, T. (1995). The eukaryotic protein kinase superfamily : kinase (catalytic) domain structure and classification. FASEB J. 9, 576-596.
110. HARA, T., KATO, H., KATSUBE, Y. & ODA, J. I. (1996). A pseudo-michaelis quaternary complex in the reverse reaction of a ligase; structure of Escherichia coli B glutathione synthetase complexed with ADP, glutathione and sulfate at 2.0-Ångstrom resolution. Biochemistry 35, 11 967-11 974.
111. HARLOS, K., VAS, M. & BLAKE, C. F. (1992). Crystal structure of the binary complex of pig muscle phosphoglycerate kinase and its substrate 3-phospho-D-glycerate. Proteins 12, 133-144.
112. HARRISON, C. J., HAYERHARTL, M., DI LIBERTO, M., HARTL, F. U. & KURIYAN, J. (1997). Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science 276, 431-435.
113. HARTL, U. (1996). Molecular chaperones in cellular protein folding. Nature 381, 571-580.
114. HASEMANN, C. A., ISTVAN, E. S., UYEDA, K. &DEISENHOFER, J. (1996). The crystal structure of the bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase reveals distinct domain homologies. Structure 4, 1017-1029.
115. HERZBERG, O., CHEN, C. C., KAPADIA, G., MCGUIRE, M., CARROLL, L. J., NOH, S. J. & DUNAWAY-MARIANO, D. (1996). Swiveling-domain mechanism tor enzymatic phosphotranster between remote reaction sites. Proc. Natl. Acad. Sci. USA 93, 2652-2657.
116. HINDS, R. M., XU, J., WALTERS, D. E. & KEMP, R. G. (1998). The active site of pyrophosphate-dependent phosphofructo-1-kinase based on site-directed mutagenesis and molecular modeling. Arch. Biochem. Biophys. 34, 47-52.
117. HIROKAWA, N. (1998). Kinesin and dynein superfamily proteins and the mechanism of organelle transport. Science 279, 519-526.
118. HOLDGATE, G. A., TUNNICLIFFE, A., WARD, W. H. J., WESTON, S. A., ROSENBROCK, G., BARTH, P. T., TAYLOR, I. W. F., PAUPTIT, R. A. & TIMMS, D. (1997). The entropic penalty of ordered water accounts for weaker binding of the antibiotic Novobiocin to a resistant mutant of DNA gyrase: a thermodynamic and crystallographic study. Biochemistry 36, 9663-9673.
119. HOLM, L. (1998). Unification of protein families. Curr. Op. Struc. Biol. 8, 372-379.
120. HOLM, L. & SANDER, C. (1995). DNA polymerase β belongs to an ancient nucleotidyltransferase superfamily. TIBS 20, 345-347.
121. HONZATKO, R. B., CRAWFORD, J. L., MONACO, H., LADNER, J. E., EDWARDS, B. F. P., EVANS, D. R., WARREN, S. G., WILEY, D. C., LADNER, R. C. & LIPSCOMB, W. N. (1982). Crystal and molecular structures of native and CTP-liganded aspartate carbamoyltransterase from Escherichia coli. J. Mol. Biol. 160, 219-263.
122. HOWARD, J. (1997). Molecular motors: structural adaptations to cellular functions. Nature 38, 561-567.
123. HU, S.-H., PARKER, M. W., LEI, J. Y., WILCE, M. C. J., BENIAN, G. M. & KEMP, B. E. (1991). Insights into autoregulation from the crystal structure ot twitchin kinase. Nature 369, 581-584.
124. HUANG, W., LINDQVIST, Y., SCHNEIDER, G., GIBSON, K., FLINT, D. & LORIMER, G. (1994). Crystal structure of an ATP dependent carboxylase, dethiobiotin synthetase, at 1.65 Ångstroms Resolution. Structure 2, 407-414.
125. HUANG, W., JIA, J., GIBSON, K. J., TAYLOR, W. S., RENDINA, A. R., SCHNEIDER, G. & LINDQVIST, Y. (1995). Mechanism of an ATP-dependent carboxylase, dethiobiotin synthetase, based on crystallographic studies of complexes with substrates and a reaction intermediate. Biochemistry 34, 10985-10995.
126. HUBBARD, S. R. (1997). Crystal structure of the activated insuline receptor tyrosine kinase in complex with peptide substrate and ATP analog. EMBO J. 16, 5572-5581.
127. HUBBARD, S. R., WEI, L., ELLIS, L. & HENDKICKSON, W. A. (1994). Crystal structure of the tyrosine kinase domain of the human insuline receptor. Nature 372, 746-754.
128. HUNG, L-W., WANG, I. X., NIKAIDO, K., LIU, P.-Q., FERRO-LUZZI AMES, G. & KIM, S.-H. (1998). Crystal structure of ATP-binding subunit of an ABC transporter. Nature 396, 703-707.
129. HUNTER, T. (1987). A thousand and one protein kinases. Cell 50, 823-829.
130. HUNTER, T. (1995). Protein kinases and phosphatases : the Yin and Yang of protein phosphorylation and signaling. Cell 80, 225-236.
131. HUNTER, T. & PLOWMAN, G. D. (1997). The protein kinases of budding yeast: six score and more. TIBS 22, 18-22.
132. HURLEY, J. H., FABER, H. R., WORTHYLAKE, D., MEADOW, N. D., ROSEMAN, S., PETTIGREW, D. W. & REMINGTON, S. J. (1993). Structure of the regulatory complex of Escherichia coli IIIGlc with glycerol kinase. Science 259, 673-677.
133. JACOBO-MOLINA, A., DING, J., NANNI, R. G., CLARK JR., A. D., LU, X., TANTILLO, C., WILLIAMS, R. L., KAMER, G., FERRIS, A. L., CLARK, P., HIZI, A., HUGHES, S. H. & ARNOLD, E. (1993). Crystal structure of human immunodeficiency virus type 1 reverse transcriptase complexed with double-stranded DNA at 3.0 Ångstroms resolution shows bent DNA. Proc. Natl. Acad. Sci. USA 90, 6230-6324.
134. JEFFREY, P. D., RUSSO, A. A., POLYAK, K., GIBBS, E., HURWITZ, J., MASSAGUÉ, J. & PAVLETICH, N. P. (1995). Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex. Nature 376, 313-320.
135. JOHNSON, L. N., NOBLE, M. H. M. & OWEN, D. J. (1996). Active and inactive protein kinases - structural basis for regulation. Cell 85, 149-158.
136. JURNAK, F. (1985). Structure of the GDP domain of EF-Tu and location of amino acids homologous to ras onco X gene proteins. Science 230, 32-36.
137. KABSCH, W. & FRITZ-WOLF, K. (1997). Mitochondrial creatine kinase - a square protein. Curr. Op. Struc. Biol. 7, 811-818.
138. KABSCH, W., MANNHERZ, H. G., SUCK, D., PAI, E. F. & HOLMES, K. C. (1990). Atomic structure of the Actin:DNase I complex. Nature 347, 37-44.
139. KIEFER, J. R., MAO, C., HANSEN, J., BASEHORE, S. L., HOGREFE, H. H., BRAMAN, J. C. & BEESE, L. S. (1997). Crystal structure of a thermostable bacillus DNA polyemrase I large fragment at 2.1 Å resolution. Structure 5, 95-108.
140. KIM, Y., EOM, S. H., WANG, J., LEE, D. S., SUH, S. W. & STEITZ, T. A. (1995). Crystal structure of Thermus aquaticus DNA polymerase. Nature 376, 612-616.
141. KLETZIN, A. (1992). Molecular characterizytion of a DNA ligase gene of the extremely thermophilic archaeon Desulfurolobus ambivalens shows close phylogenetic relationship tp eukaryotic ligases. Nucl. Acids Res. 20, 5389-5396.
142. KNIGHTON, D. R., ZHENG, J., TEN EYCK, L. F., ASHFORD, V. A., XUONG, N.-H., TAYLOR, S. S. & SOWADSKI, J. M. (1991). Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253, 407-414.
143. KNOWLES, J. R. (1980). Enzyme-catalyzed phosphoryl transfer reactions. Ann. Rev. Biochem. 49, 877-919.
144. KOHLSTAEDT, L. A., WANG, J., FRIEDMAM, J. M., RICE, P. A. & STEITZ, T. A. (1992). Crystal structure at 3.5 Å resolution of HIV-1 reverse transcriptase complexed with an inhibitor. Science 256, 1783-1790.
145. KOMOSZYNSKI, M. & WOJTCZAK, A. (1996). Apyrases (ATP diphosphohydrolases, EC 3.6.1.5): function and relationship to ATPases. Biocchim. Biophys. Acta 1310, 233-241.
146. KOONIN, E. V. &: RUDD, K. E. (1996). The two domains of superfamily I helicases may exist as separate proteins Protein Science 5, 178-180.
147. KOROLEV, S., NAYAL, M., BARNES, W. M., DI CERA, E. & WAKSMAN, G. (1995). Crystal structure of the large fragment of Thermus aquaticus DNA polymerase I at 2.5-A resolution: structural basis for thermostability. Proc. Natl. Acad. Sci. USA 92, 9264-9268.
148. KOROLEV, S., HSIEH, J., GAUSS, G. H., LOHMAN, T. M. & WAKSMAN, G. (1997). Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-strnded DNA and ADP. Cell 90, 635-647.
149. KULL, F. J., SABLIN, E. P., LAU, R., FLETTERICK, R. J. & VALE. R. D. (1996). Crystal structure of the kinesin motor domain reveals a structural similarity to myosin. Nature 380, 550-555.
150. KUNAU, W. H., BEYER, A., FRANKEN, T , GOTTE, K., MARZIOCH, M., SAIDOWSKI, J., SKALETZ-ROROWSKI, A. & WIEBEL, F. (1993). Two complementary approaches to study peroxisome biogenesis in Saccharomyces cerevisiae : forward and reversed genetics. Biochimie 75, 209-224.
151. KUTZENKO, A. S., LAMZIN, V. S. & POPOV, V. O. (1998). Conserved supersecondary structural motif in NAD-dependent dehydrogenases. FEBS Lett. 423, 105-109.
152. LACOUR, T. F. M., NYBORG, J., THIRUP, S. & CLARK, B. F. C. (1985). Structural details of the binding of guanosine diphosphate to elongation factor Tu from E. coli as studied by X-ray crystallography. EMBO J. 4, 2385-2388.
153. LADROR, U. S., GOLLAPUDI, L., TRIPATHI, R. L., LATSHAW, S. P. & KEMP, R. G. (1991). Cloning, sequencing, and expression of pyrophosphate-dependent phosphofructokinase from Propionibacterium freudenreichii. J. Biol. Chem. 266, 16550-16555.
154. + and pyruvate. Biochemistry 33, 63101-6309.
155. + and L - phospholactate at 2.7 À resolution. Arch. Biochem. Biophys. 345, 199-206.
156. LARSSON, G., SVENSSON, L. A. & NYMAN, P. O. (1996). Crystal structure of the Escherichia coli dUTPase on complex with a substrate analogue (dUDP). Nature Struc. Biol. 3, 532-538.
157. LARSSON-RAZNIKIEWICZ, M. M. (1973). Graphical analyses on binding of ligands to a two-sited system. Theoretical treatments exemplified on yeast phosphoglycerate kinase. Arch. Biochem. Biophys. 158, 754-762.
158. LAVIE, A., VETTER, I. R., KONRAD, M., GOODY, R. S., REINSTEIN, J. & SCHLICHTUNG, I. (1997). Structure of thymidylate kinase reveals the cause behind the limiting step in AZT activation, Nature Structural Biology 4, 601-604.
159. LEATHERBARROW, R. J., FERSHT, A. R. & WINTER, G. (1985). Transition-state stabilization in the mechanism of tyrosyl-tRNA synthetase revealed by protein engineering. Proc. Natl. Acad. Sci. USA 82, 7840-7844
160. LENZEN, C. U., STEINMANN, D., WHITEHEART, S. W. & WEIS, W. I. (1998). Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein. Cell 94, 525-536.
161. LEW, J., TAYLOR, S. S. & ADAMS, J. A. (1997). Identification of a partially rate-determining step in the catalytic mechanism of cAMP-dependent protein kinase - a transient kinetic study using stopped-flow fluorescence spectroscopy. Biochemistry 36, 6717-6724.
162. LIAW, S. H., PAN, C. & EISENBERG, D. (1993). Feedback inhibition of fully unadenylated glutamine synthetase from Salmonella typhimurium by glycine, alanine and serine, Proc. Natl. Acad. Sci. USA 90, 4996-5000.
163. LIAW, S.-H., JUN, G. & EISENBERG, D. (1994). Interaction of nucleotides with fully unadenylated glutamine synthetase from Salmonella typhimurium. Biochemistry 33. 11184-11188.
164. LIAW, S. H., KUO, I. C. & EISENBERG, D. (1995). Discovery of the ammonium substrate site on glutamine synthetase, a third cation binding site. Protein Science 4, 2358-2365.
165. LIMA, C. D., WANG, J. C. & MONDRAGON, A. (1994). Three-dimensional structure of the 67k N-terminal fragment of E. coli DNA topoisomerase I. Nature 367, 138-146.
166. 2+ Complex and Mechanism of its Pyrophosphohydrolase Action. Biochemistry 36, 1199-1211.
167. LINDNER, P., LASKO, P. F., LEROY, P., NIELSEN, P. J., NISHI, K., SCHNIER, J. & SLONIMSKI, P. P. (1989). Birth of the D-E-A-D box. Nature 337, 121-122.
168. LINTON, K. J. & HIGGINS, C. F. (1998). The Escherichia coli ATP-binding cassette (ABC) proteins, Molec. Microbiol. 28, 5-13.
169. LLORCA, O., MARCO, S., CARRASCOSA, J. L. & VALPUESTA, J. M. (1997). Conformational changes in the GroEL oligomer during the functional cycle. J. Struc. Biol. 118, 31-42.
170. LOEWE, J. & AMOS, L. A. (1998). Crystal structure of the bacterial cell-division protein FtsZ. Nature 391, 203-206.
171. LOGAN, D. T., MAZAURIC, M.-H., KERN, D. & MORAS, D. (1995). Crystal structure of glycyl-tRNA synthetase from T. thermophilus. EMBO J. 14, 4156-416.
172. LUE, N., SHARMA, A., MONDRAGON, A & WANG, J. C. (1995). A 25kDa yeast DNA topoisomerase I fragment: crystallographic structure and mechanistic implications. Structure 3, 1315-1322.
173. MARKHAM, G. D., HAFNER, E. W., TABOR, C. W. & TABOR, H. (1980). S-Adenosylmethionine synthetase from Escherichia coli. J. Biol. Chem. 255, 9082-9092.
174. MATSUDA, K., MIZUGUCHI, K., NISHIOKA, T., KATO, H., GO, N. & ODA, J. (1996). Crystal structure of gluthathione synthetase at optimal pH: domain architecture and structural similarity with other proteins. Protein Engineering 9, 1083-1092.
175. MATTE, A., GOLDIE, H., SWEET, R. M. & DELBAERE, L. T. (1996). Crystal structure of Escherichia coli phosphoenolpyruvate carboxykinase: a new structural family with the P-loop nucleoside triphosphate hydrolase fold. J. Mol. Biol. 256, 126-143.
176. MATTE, A., TARI, L. W., GOLDIE, H. & DELBAERE, L. T. (1997). Structure and mechanism of phosphoenolpyruvate carboxykinase, J. Biol. Chem. 272, 8105-8108.
177. MATTEVI, A., VALENTINI, G., RIZZI, M., SPERANZA, M. L., BOLOGNESI, M. & CODA, A. (1995). Crystal structure of Escherichia coli pyruvate kinase type I: molecular basis of the allosteric transition. Structure 3, 729-741.
178. MAYANS, O., VAN DER VEN, P. F. M., WILM, M., MUES, A., YOUNG, P., FÜRST, D. O., WILMANNS, M. & GAUTEL, M. (1998). Structural basis for activation of the titin kinase domain during myofibrillogenesis. Nature 395, 863-869.
179. MCPHILLIPS, T. M., HSU, B. T., SHERMAN, M. A., MAS, M. T. & REES, D. (1996). Structure of the R65Q mutant of yeast 3-phosphoglycerate kinase complexed with Mg-AMP-PNP and 3-phospho-D-glycerate. Biochemistry 35, 4118-4127.
180. MILBURN, M. V., TONG, L., DEVOS, A. M., BRÜNGER, A., YAMAIZUMI, Z., NISHIMURA, S. & KIM, S.-H. (1990). Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic ras proteins. Science 247, 939-945.
181. MILDVAN, A. S. (1970). In The Enzymes (ed. P. D. Boyer). 3rd Edn, pp. 445 536. Academic Press, New York.
182. MILNER-WHITE, E. J., COGGINS, J. R. & ANTON, I. A. (1991). Evidence for an ancestral core structure in nucleotide-binding proteins with the type A motif. J. Mol. Biol. 221, 751-754.
183. MOHAMMADI, M., SCHLESSINGER, J. & HUBBARD, S. R. (1996). Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism. Cell 86, 577-587.
184. MOHAMMADI, M., MCMAHON, G., SUN, L., TANG, C., HIRTH, P., YEH, B. K., HUBBARD, S. R. & SCHLESSINGER, J. (1997). Structures Of the tyrosine kinase domain of fibroblast growth factor receptor in complex with inhibitors. Science 276, 955-960
185. MOLLER, J. V., JUUL, B. & LE MAIRE, M. (1996). Structural organisation, ion transport, and energy transduction of P-type ATPases. Biochim. Biophys. Acta. 1286, 1-51.
186. MONTOYA, G., SVENSSON, C., LUIRINK, J. & SINNING, I. (1997). Crystal structure of the NG domain from the signal-recognition particle receptor Fts Y. Nature 385, 365-368.
187. MORÉRA, S., LASCU, I., DUMAS, C., LEBRAS, G., BRIOZZO, P, VÉRON, M. & JANIN, J. (1994). Adenosine 5′-diphosphate binding and the active site of nucleoside diphosphate kinase. Biochemistry 33, 459 467.
188. MORÉRA, S., CHIADMI, M., LEBRAS, G., LASCU, I. & JANIN, J. (1995). Mechanism of phosphate transfer by nucloeside diphosphate kinase: X-ray structures of the phosphohistidine intermediate of the enzymes from Drosophila and Dictyostelium. Biochemistry 34, 11 062-11 070.
189. MOSYAK, L., RESHETNIKOVA, L., GOLDGUR, Y., DELARUE, M. & SAHRO, M. G. (1995). Structure of phenylalanyl-tRNA synthetase from T. thermophilus. Nat. Struc. Biol. 2, 537-547.
190. 5A refined at 1.9 Å resolution. A model for a catalytic transition state. J. Mol. Biol. 224, 159-177.
191. MÜLLER-DIECKMANN, H. J. & SCHULZ, G. E. (1994). The structure of uridylate kinase with its substrates: Geometry of the phosphoryl transfer transition state. J. Mol. Biol. 236, 361-367.
192. MURZIN, A. G. (1996). Structural classification of proteins: new superfamilies. Curr. Op. Struct. Biol. 6, 386-394.
193. MURZIN, A. G., BRENNER, S. E., HUBBARD, T. & CHOTHIA, C. (1995). SCOP: A structural classification of protein database for the investigation of sequences and structures. J. Mol. Biol. 247, 536-540.
194. NAKATSU, T., KATO, H. & ODA, J. (1998). Crystal structure of asparagine synthetase reveals a close evolutionary relationship to Class II tRNA synthetase. Nature Struct. Biol. 5, 15-19.
195. - 3p14.2 is abnormal in breast carcinomas. Cancer Res. 56, 3173-3179.
196. NIEFIND, K., GUERRA, B., PINNA, L. A., ISSINGER, O.-G. & SCHOMBURG, D. (1998). Crystal structure of the catalytic subunit of protein kinase CK2 from Zea mays at 2.1 Å resolution. EMBO J. 17, 2451-2462.
197. NOEL, J. P , HAMM, H. E. & SIGLER, P. B. (1993). The 2.2 Å crystal structure of transducin-α complexed with GTPγS. Nature 366, 654-663.
198. NOGALES, E., WOLF, S. G. & DOWNING, K. H. (1998a). Structure of the ab tubulin dimer by electron crystallography. Nature 391, 199-203.
199. NOGALES, E., DOWNING, K. H., AMOS, L. A. & LOWE, J. (1998b). Tubulin and FtsZ form a distinct family of GTPases. Nat. Struc. Biol. 5, 451-458.
200. NUREKI, O., VASSYLYEV, D. G., KATAYANAGI, K., SHIMIZU, T., SEKINE, S., KIGAWA, T., MUYAZAWA, T., YOKOYAMA, S. & MORIKAWA, K. (1995). Architectures of class-defining and specific domains of glutamyl-tRNA synthetase. Science 267, 1958-1965.
201. NUREKI, O., VASSYLYEV, D. G., TATENO, M., SHIMADA, A., NAKAMA, T., FUKAI, S., KONNO, M., HENDRICKSON, T. L., SCHIMMEL, P. & YOKOYAMA, S. (1998). Enzyme structure with two catalytic sites for doublesieve selection of substrate. Science 280, 578-582,
202. OLLIS, D. L., BRICK, P., HAMLIN, R., XUONG, N. G. & STEITZ T. A. (1985). Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP. Nature 313, 762-766.
203. ONESTI, S., MILLER, A. D. & BRICK, P. (1995). The crystal structure of the lysyl-tRNA synthetase (LysU). from Escherichia coli. Structure 3, 163-176.
204. OWEN, D. J., NOBLE, M. E.M, GARMAN, E. F., PAPAGEORGIOU, A. C. & JOHNSON, L. N. (1995). Two structures of the catalytic domain of phosphorylase kinase: an active protein kinase complexed with substrate analogue and product. Structure 3, 467-482.
205. PACE, H. C., GARRISON, P. N., ROBINSON, A. K., BARNES, L. D., DRAGANESCU, A., RÖSLER, A., BLACKBURN, G. M., SIPRASUVILI, Z., CROCE, C. M., HUEBNER, K. & BRENNER, C. (1998). Genetic, biochemical and crystallographic characterization of Fhit-substrate complexes as the active signaling form of Fhit. Proc. Natl. Acad. Sci. 95, 5484-5489.
206. PAI, E. F., KRENGEL, U., PETSKO, G. A., GOODY, R. S., KABSCH, W. & WITTINGHOFER, A. (1990). Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 Å resolution: implications for the mechanism of GTP hydrolysis. EMBO J. 9, 2351-2359.
207. PARSELL, D. A., SANCHEZ, Y., STITZEL, J. D. & LINDQUIST, S. (1991). Hsp104 is a highly conserved protein with two essential nucleotide binding sites. Nature 353, 270-273.
208. PATEL, S. & LATTERICH, M. (1998), The AAA team: related ATPases with diverse functions. Trends in Cell Biology 8, 65-71.
209. PEDERSEN, L. C., BENNING, M. M. & HOLDEN, H. M. (1995). Structural investigation of the: antibiotic and ATP-binding sites in kanamycin nucleotidyltransferase. Biochemistry 34, 13305-13311.
210. PELLETIER, H., SAWAYA, M. R., KUMAR, A., WILSON, S. H. & KRAUT, J. (1994) Structures of ternary complexes of rat DNA polymerase β, a DNA template-primer, and ddCTP. Science 266, 2025-2026.
211. PELLETIER, H., SAWAYA, M. R., WOLFLE, W., WILSON, S. & KRAUT, J. (1996). Crystal structures of human DNA polymerase β complexed with DNA: implications for catalytic mechanism, processivity and fidelity. Biochemistry 35, 12742-12761.
212. PERONA, J., ROULD, M. A. & STEITZ. T. A. (1993). Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase. Biochemistry 32, 8758-8771.
213. POLAND, B. W., SILVA, M. M., SERRA, M. A., CHO, Y., KIM, K. H., HARRIS, E. M. S. & HONZATKO, R. B. (1993). Crystal structure of adenylosuccinate synthetase from Escherichia coli. J. Biol. Chem. 268, 25334-25342.
214. POLAND, B. W., HOU, Z., BRUNS, C., FROMM, H. J. & HONZATKO, R. B. (1996). Refined crystal structure of guanine nucleotide complexes of adenylosuccinate synthase from Escherichia coli. J. Biol. Chem. 271, 15407-15413.
215. PRODROMOU, C., ROE, S. M., PIPER, P. W. & PEARL, L. H. (1997a). A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone. Nature Struc. Biol. 4, 477-482.
216. PRODROMOU, C., ROE, S. M., O'BRIEN, R., LADBURY, J. E., PIPER, P. W. & PEARL, L. H. (1997b). Identification and characterization of the ATP/ADP binding site in the Hsp90 molecular chaperone. Cell 90, 65-75.
217. 31P NMR study of bound reactants and products of yeast 3-phosphoglycerate kinase at equilibrium and the effect of sulfate ion. J. Biol. Chem. 253, 8056-8060
218. RAUSHEL, F. M., THODEN, J. B., REINHART, G. D. & HOLDEN, H.M. (1998). Carbamoyl phosphate synthetase a crooked path from substrates to products. Curr. Op. Chem. Biol. 2, 624-632.
219. 31P NMR studies of enzyme-bound substrate complexes of yeast 3-phosphoglycerate kinase. 1. Effects of sulfate and pH. Mg(II) affinity at the two ATP sites. Biochemistry 27, 5574-5578
220. RAYMENT, L, RYPNIEWSKI, W. R., SCHMIDT-BÄSE, K., SMITH, R., TOMCHICK, D. R., BENNING, M. M., WINKELMANN, D. A., WESENBERG, G. & HOLDEN, H. M. (1993). Three-dimensional structure of myosin subfragment-1 : a molecular motor. Science 261, 50-65.
221. REDINBO, M. R., STEWART, L., KUHN, P., CHAMPOUX, J. J. & HOL, W. G. J. (1998). Crystal structure of human topoisomerase I in covalent and noncovalent complexes with DNA. Science 279, 1504-1513.
222. REN, J., ESNOUF, R., HOPLINS, A., Ross, C., JONES, Y., STAMMERS, D. & STUART, D. (1995). The structure of HIV-1 reverse transcriptase complexed with 9-chloro-TIBO: lessons for inhibitor design. Structure 3, 915-926.
223. RIORDAN, J. R., ROMMENS, J. M., KEREM, B.-S., ALON, N., ROZMAHEL, R., GRZELCZAK, Z., ZIELENSKI, J., LOK, S., PLAVSIC, N., CHOU, J.-L., DRUMM, M. L., IANNUZZI, M. C., COLLINS, F. S. & TSUI, L.-C. (1989). Identification of the cystic fibrosis gene: cloning and characterization of complementary DNA. Science 245, 1065-1073.
224. RITTINGER, K., WALKER, P. A., ECCLESTON, J. F., NURMAHOMED, K., OWEN, D., LAUE, E., GAMBLIN, S. J & SMERDON, S. J. (1997a). Crystal structure of a small G protein in complex with the GTPase activating protein RHOGAP. Nature 388, 693-697.
225. RITTINGER, K., WALKER, P. A., ECCLESTON, J. F., SMERDON, S. J. & GAMBLIN, S. J. (1997b). Structure at 1.65 A of RhoA and its GTPase-activating protein in complex with a transition-state analogue. Nature 389, 758-762.
226. RIZZI, M., NESSI, C., MATTEVI, A., CODA, A., BOLOGNESI, M. & GALIZZI, A. (1996). Crystal structure of NH3-dcpcndent NAD+ synthetase from Bacillus subtilis. EMBO J. 15, 5125-5134.
227. ROCA, J. R. & WANG, J. C. (1992). The capture of a DNA double helix by an ATP-dependent protein clamp: a key step in DNA transport by type II DNA topoisomerases. Cell 71, 833-840.
228. ROCA, J. & WANG, J. C. (1994). DNA transport by a type II DNA topoisomerase: evidence in favor of a two-gate mechanism. Cell, 609-616.
229. RODGERS, D. W., GAMBLIN, S. J., HARRIS, B. A., RAY, S., CULP, J. S., HELLMIG, B., WOOLF, D. J., DEBOUCK, C. & HARRISON, S. C. (1995). The structure of unliganded reverse transcriptase from the human immunodeficiency virus type 1. Proc. Natl. Acad. Sci. USA 92, 1222-1226.
230. ROSEMAN, A. M., CHEN, S., WHITE, H., BRAIG, K. & SAIBIL., H. R. (1996). The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL. Cell 87, 241-251.
231. ROTHMAN, J. E. (1994). Mechanisms of intracellular protein transport. Nature 372, 55-63
232. ROULD, M., PERONA, J.J. & STEITZ, T. A. (1989). Structure of Escherichia-coli glutaminyl transfer RNA synthetase complexed with glutaminyl transfer RNA and ATP at 2.8 Å resolution. Science 246, 1135-1142.
233. ROSSMANN, M. G., LILJAS, A., BRÄNDEN, C.-I. & BANASZAK, L. J. (1975). Evolutionary and structural relationships among dehydrogenases. In: The Enzymes (ed. P. D. Boyer), vol. 11, 3rd edn, pp. 61-102. Academic Press, New York.
234. Asp. Science 252, 1682-1689.
235. Kipl cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 diplex. Nature 382, 325-331.
236. RYPNIEWSKI, W. R. & EVANS, P. R. (1989). Crystal structure of unliganded phosphofructokinase from Escherichia coli. J. Mol. Biol. 207, 805-821.
237. SACK, S., MULLER, J., MARX, A., THORMAHLEN, M., MANDELKOW, E. M., BRADY, S. T. & MANDELKOW, E. (1997). X-ray structure of motor and neck domains from rat brain kinesin. Biochemistry 36, 16155-16165.
238. SAKON, J., LIAO, H. H., KANIKULA, A.M., BENNING, M. M., RAYMENT, I. & HOLDEN, H.M. (1993). Molecular structure of kanamycin nucleotidyltransferase determined to 3.0 Å resolution, Biochemistry 32, 11977-11984.
239. SARASTE, M., SIBBALD, P. R. & WITTINGHOFER, A. (1990). The P-loop - A common motif in ATP and GTP binding proteins. Trends Biochem. Sci. 15, 430-434.
240. SAVAGE, H., MONTOYA, G., SVENSSON, C., SCHWENN, J.D. & SINNING, I. (1997). Crystal structure of phosphoadenyl sulphate (PAPS) reductase: a new family of adenine nucleotide α hydrolases. Structure 5, 895-906.
241. SAWAYA, M. R., PELLETIER, H., KUMAR, A., WILSON, S. H. & KRAUT, J. (1994). Crystal structure of rat DNA polymerase β: evidence for a common polymerase mechanism. Science 264, 1930-1935.
242. 2- at 2.2 Å: implications for water-mediated specificity. Biochemistry 35, 9716.
243. SCHEFFZEK, K., LAUTWEIN, A., KABSCH, W., AHMADIAN, M. R. & WITTINGHOFER, A. (1996b). Crystal structure of the GTPase-activating domain of human p120GAP and implications for the interaction with Ras. Nature 384, 591-596
244. SCHEFFZEK, K., AHMADIAN, M. R., KABSCH, W., WIESMULLER, L., LAUTWEIN, A., SCHMITZ, F. & WITTINGHOFER, A. (1997). Ras-RasGAP communication: structural basis for GTPase activation and its loss in oncogenic Ras mutants. Science 277, 333-338.
245. SCHIERBECK, B. & LARSSON-RAZNIKTFAVICZ, M. (1979). Product inhibition studies of yeast phosphoglycerate kinase evaluating properties of multiple substrate binding sites. Biochim. Biophys. Acta. 568, 195-204.
246. SCHINDELIN, N., KISKER, C., SCHLESSMAN, J. L., HOWARD, J. B. & REES, D. C. (1997). Structure of ADP· AlF(4)(-)-stabilized nitrogenase complex and its implications for signal transduction. Nature 387, 370 376.
247. SCHLICHTING, I. & REINSTEIN, J. (1997). Structure of active conformations of UMP kinase from Dictyostelium discoideum suggest phosphoryl transfer is associative. Biochemistry 36, 9290-9296.
248. SCHIRMER, T. & EVANS, P. R. (1990). Structural basis of the allosteric behaviour of phospnofructokinase. Nature 343, 140-145.
249. SCHMIDT, M., RUTKAT, K., RACHEL, R., PFEIFER, G., JAENICKE, R., VIITANEN, P., LORIMER, G. & BUCHNER, J. (1994). Symmetric complexes of GroE chaperonins as part of the functional cycle. Science 265, 656-659.
250. SCHWEINS, T. & WITTINGHOFER, A. (1994). Structures, interactions and relationships. Current Biology 4, 547-550.
251. SCHWEINS, T., GEYER, M., SCHEFFZEK, K., WARSHEL, A., KALBITZER, H. R. & WITTINGHOFER A. (1995). Substrate-assisted catalysis as a mechanism for GTP hydrolysis of p21ras and other GTP-binding proteins. Nature Structural Biology 2, 36-44.
252. SCHWEINS, T., GEYER, M., KALBITZER, H. R., WITTINGHOFER, A. & WARSHEL, A. (1996). Linear free energy relationships in the intrinsic and GAP activating protein-stimulated guanosine 5′-triphosphate hydrolysis of p21ras. Biochemistry 35, 14225-14231.
253. SCHULZ, G. (1992). Binding of nucleotides by proteins. Current Op. Struct. Biol. 2, 61-67.
254. SCHULZ, G. E., ELZINGA, M., MARX, F & SCHIRMER, R. H. (1974). Three-dimensional structure of adenylate kinase. Nature 250, 120-123.
255. SCHULZ, G. E., MÜLLER, C. W. & DIEDERICHS, K. (1990). Induced-fit movements in adenylate kinases. J. Mol. Biol. 213, 627-630.
256. SCHULTZ, P, OLLAND, S., OUDET, P. & HANCOCK, R. (1996). Structure and conformational changes of DNA topoisomerase II visualized by electron microscopy. Proc. Natl. Acad. Sci. USA 93,
257. SCHULZE-GAHMEN, U., DE BONDT, H. L. & KIM, S.-H. (1996). High resolution crystal structures of human cyclin-dependent kinase 2 with and without ATP: bound waters and natural ligand as guides for inhibitor design. Journal of Medicinal Chemistry 39, 4540-4506.
258. SCOPES, R. K. (1978). Binding of substrates and other anions to yeast phosphoglycerate kinase. Eur. J. Biochem. 91, 119-129.
259. SHARMA, A., HAUAI, R. & MONDRAGON, A. (1994). Crystal structure of the amino-terminal fragment of vaccinia virus DNA topoisomerase 1 at 1.6 Å resolution. Structure 2, 767-777.
260. SHIRAKIHARA, Y. & EVANS, P. R. (1988). Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction products. J. Mol. Biol. 204, 973-994.
261. SHUMAN, S. (1996). Closing the gap on DNA ligase. Structure 4, 653-656.
262. SICHERI, F., MOAREFI, I. & KURIYAN, J. (1997). Crystal structure of the Src family tyrosine kinase Hck. Nature 385, 602-609.
263. SICHERIE, F. & KURIYAN, J. (1997). Structures of Src-family tyrosine kinases. Curr. Op. Struc. Biol. 7, 777-785.
264. SILVA, M. M., POLAND, B. W., HOFFMANN, C. R., FROMM, H.J. & HONZATKO, R.B. (1995). Refined crystal structures of unligated adenylosuccinate synthetase from Escherichia coli. J. Mol. Biol. 254, 431-446.
265. SMITH, C. A. & RAYMENT, I. (1996). X-ray structure of the magnesium(II)· ADP· Vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 Å Resolution. Biochemistry 35, 5404-5417.
266. SMITH, K. E. & FISHER, M. T. (1995). Interactions between the GroE chaperonins and rhodanese. Multiple intermediates and release and rebinding. J. Biol. Chem. 270, 21517-21523.
267. 4. Nature 372, 276-279.
268. SOUSA, R. (1996). Structural and mechanistic relationships between nucleic acid polymerases. TIBS 21, 186-190.
269. SOUSA, R., CHUNG, Y. J., ROSE, J. P. & WANG, B. C. (1993). Crystal structure of bacteriophage T7 RNA polymerase at 3.3 Å resolution. Nature 364, 593-599.
270. SOZZI, G., VERONESE, M. L., NEGRINI, M., BAFFA, R., COTTICELLI, M. G., INOUE, H., TORNIELLI, S., PILOTTI, S., DR GREGORIO, L., PASTORINI, U., PIEROTTI, M. A., OHTA, M., HUEBNER, H. & CROCE, C M. (1996). The FHIT gene 3p14.2 is abnormal in lung cancer. Cell 85, 17-26.
271. SOZZI, G., SARD, L., DE GREGORIO, L., MARCHETTI, A., MUSSO, K., BUTTITTA, F., TORNIELLI, S., PELLEGRINI, S., VERONESE, M. L., MANENTI, G., INCARBONE, M., CHELLA, A., ANGELETTI, C. A., PASTORINO, U., HUEBNER, K., BEVILAQUA, G., PILOTTI, S., CROCE, C. M. & PIEROTTI, M. A. (1997a). Association between cigarette somking and FHIT gene alterations in lung cancer. Cancer Res. 57, 2121-2123.
272. SOZZI, G., TORNIELLI, S., TAGLIABUE, E., SARD, L., PEZZELLA, F., PASTORINI, U., MINOLETTI, F., PILOTTI, S., RADCLIFFE, C., VERONESE, M. L., GOLDSTRAW, P., HUEBNER, K., CROCE, C. M. & PIEROTTI, M. A. (1997b). Absence of Fhit protein in primary lung tumors and cell lines with FHIT gene abnormalities. Cancer Res. 57, 5207-5212.
273. STEHLE, T. & SCHULZ, G. E. (1992). Refined structure of the complex between guanylate kinase and its substrate GMP at 2.0 Å resolution. J. Mol. Biol. 224, 1127-1141.
274. STEITZ, T. A. (1998), A mechanism for all polymerases. Nature 391, 231-232.
275. STEITZ, T. A., SHOHAM, M. & BENNETT, W. S. (1981). Structural dynamics of yeast hexokinase during catalysis. Phil. Trans. R. Soc. London 293, 43-52.
276. STEITZ, T. A. & STEITZ, J. A. (1993). A general two-metal-ion mechanism for catalytic RNA. Proc. Natl. Acad. Sci. USA 90, 6498-6502.
277. STEVES, R. C., GOUAUX, J. E. & LIPSCOMB, W. N. (1990). Structural consequences of effector binding to the T state of aspartate carbamoyltransferase. Crystal structures of the unligated and ATP-, and CTP-complexed enzymes at 2.6-ångstrom resolution. Biochemistry 29, 7691-7701.
278. STEWART, L., REDINBO, M. R., QIU, X., HOL, W. G. J. & CHAMPOUX, J. J. (1998). A model for the mechanism of human topoisomerase I. Science 279, 1534 1541.
279. STORY, R. M., WEBER, I. T. & STEITZ, T. A. (1992). Structure of the recA protein-ADP complex. Nature 355, 374-376.
280. STORY, R. M. & STEITZ, T. A. (1992). The structure of the E. coli RecA protein monomer and polymer. Nature 355, 318-325.
281. STRÄTER, N., LIPSCOMB, W. N., KLABUNDE, T. & KREBS, B. (1996). Two-metal ion catalysis in enzymatic acyl- and phosphoryl-transfer reactions. Angewandt Chemie / International Edition in English 35, 2024-2055.
282. STUART, D. I., LAVINE, M., MUIRHEAD, H. & STAMMERS, D. K. (1979). Crystal structure of cat muscle pyruvate kinase at a resolution of 2.6 Ångstroms. J. Mol. Biol. 134, 109-142.
283. SUBRAMANYA, H. S., BIRD, L. E., BRANNIGAN, J. A. & WIGLEY, D. B. (1996a). Crystal structures of DExx box helicase. Nature 384, 379-383.
284. SUBRAMANYA, H. S., DOHERTY, A. J., ASHFORD, S. R. & WIGLEY, D. B. (1996b). Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7. Cell 85, 607-615.
285. SUZUKI, C. K., REP, M., VAN DIJL, J. M., SUDA, K., GRIVELL, L. A. & SCHATZ, G. (1997). ATP-dependent proteases that also chaperone protein biogenesis. TIBS 22, 118-123.
286. TAKUSAGAWA, F., KAMITORI, S. & MARKHAM, G. D. (1996). Structure and function of S-adenosylmethionine synthetase with ADP, BrADP, and PPi at 2.8 Å resolution. Biochemistry 35, 2586-2596.
287. TAMPÉ, R. (1998). Das 'ABC' der Immunologie-Funktion des Peptid-Transportkomplexes TAP bei der zellulären Immunerkennung. Biospektrum 1, 23 28.
288. TANAKA, T., SAHA, S. K., TOMOMORI, C., ISHIMA, R., LIN, D., TONG, K. I., PARK, H., DUTTA, R., QUIN, L., SWINDELL, S. M. B., YAMAZAKI, T., ONO, A. M., KAINOSHO, M., INOUYE, M. & IKURA, M. (1998). NMR structure of the histidine kinase domain of the E. coli osmosensor EnvZ. Nature 396, 88-92.
289. TANG, W. J. & GILMAN, A. G. (1995). Construction of a soluble adenylyl cyclase activated by G(S)Alpha and forskolin. Science 268, 1769-1772.
290. 2--oxalate ternary complex of Escherichia coli PEP carboxykinase. Nat. Struct. Biol. 3, 355-363.
291. TAYLOR, S. S., KNIGHTON, D. R., ZHENG, J., SOWADSKI, J. M., GIBBS, C. S. & ZOLLER, M. J. (1993). A template for the protein kinase family. TIBS 18, 84-89.
292. TAYLOR, S. S. & RADZIO-ANSELM, E. (1994). Three protein kinase structures define a common motif. Structure 2, 345-355.
293. TEPLYAKOV, A., SEBASTIAO, P., OBMOLOVA, G., PERRAKIS, A., BRUSH, G. S., BESSMAN, M. J. & WILSON, K. S. (1996). Crystal structure of bacteriophage T4 deoxynucleotide kinase with its substrates dGMP and ATP. EMBO J. 15, 3487-3497.
294. TESMER, J. J. G., KLEM, T. J., DERAS, M. L., DAVISSON, V. J. & SMITH, J. L. (1996). The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families. Nature Struct. Biol. 3, 74-86.
295. Sx· GTPγS. Science 278, 1907-1916.
296. TESMER, J. J. G., SUNAHARA, R. K., JOHNSON, R. A., GOSSELIN, G., GILMAN, A. G. & SPRANG, S. R. (1999). Two-metal-ion catalysis in adenylyl cyclase. Science 285, 756-760.
297. THE C. ELEGANS SEQUENCING CONSORTIUM. (1998). Genome sequence of the nematode C. elegans : a platform for investigating biology. Science 282, 2012-2018.
298. THEYSSEN, H., SCHUSTER, H. -P., PACKSCHIES, L., BUKAU, B. & REINSTEIN, J. (1996). The second step of ATP binding to DnaK induces peptide release. J. Mol. Biol. 263, 657-670.
299. THODEN, J. B., HOLDEN, H. M., WESENBERG, G., RAUSHELM, F. M. & RAYMENT, I. (1997). Structure of carbamoyl phosphate synthetase: a journey of 96 Å from substrate to product. Biochemistry 36, 6305-6316.
300. TSAI, F. T. F., SINGH, O. M. P., SKARZYNSKI, T., WONACOTT, A. J., WESTON, S., TUCKER, A., PAUPTIT, R. A., BREEZE, A. L., POYSER, J. P., O'BRIEN, R. O., LADBURY, J. E. & WIGLEY, D. B. (1997). The highresolution crystal structure of a 24 kDa gyrase B fragment from E. coli complexed with one of the most potent coumarin inhibitors, Chlorobiocin. Proteins 28, 41-52.
301. TSAI, M.-D. & YAN, H. (1991). Mechanism of adenylate kinase: site-directed mutagenesis versus X-ray and NMR. Biochemistry 30, 6806-6818.
302. TRAUT, T. W. (1994). The functions and consensus motifs of nine types of peptide segments that form different types of nucleotide-binding sites. Eur. J. Biochem. 222, 9-19.
303. VALENZUELA, J. G., CHARLAB, R., GALPERIN, M. Y. & RIBEIRO, J. M. C. (1998). Purification, cloning, and expression of an apyrase from the bed bug Cimex lectularius. J. Biol. Chem. 273, 30583-30590.
304. VIRGILIO, L., SCHUSTER, M., GOLLIN, S. M., VERONESE, M. L., OHTA, M., HUEBNER, K. & CROCE, C. M. (1996). FHIT gene alteration in head and neck squamous cell carcinomas. Proc. Natl. Acad. Sci USA 93, 9770-9775.
305. VOLZ, K. & MATSUMURA, P. (1991). Crystal structure of Escherichia coli CheY refined at 1.7-Ångstrom resolution. J. Biol. Chem. 266, 15511-15519.
306. VONRHEIN, C., SCHLAUDERER, G. J. & SCHULZ, G. W. (1995). Movie of the structural changes during a catalytic cycle of nucleoside monophosphate kinases. Structure 3, 483-490.
307. WALDROP, G. L., RAYMENT, I. & HOLDEN, H. M. (1994). Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase. Biochemistry 33, 10249-10256.
308. WALKER, J. E., SARASTE, M., RUNSWICK, M. J. & GAY, N.J. (1982). Distantly related sequences in the alpha-and beta-subunits of ATP synrhase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1, 945-951.
309. WANG. J. C. (1996). DNA topoisomerases. Annu. Rev. Biochem. 65, 635-692.
310. WANG, J., SATTAR, A. K. M. A., WANG, C. C, KARAM, J. D., KONIGSBERG, W. H. & STEITZ, T. A. (1997). Crystal structure of a pol α. replication DNA polymerase from bacteriophage RB69. Cell 89, 1089-1098.
311. WASSARMAN, D. A. & STEITZ, J. A. (1991). Alive with DEAD proteins. Nature 349, 463-464.
312. WATENPAUGH, K. D., SIEKER, L. C., JANSEN, L. H., LEGALL, J. & DUBOURDIEU, M. (1972). Structure of the Oxidized form of a Flavodoxin at 2.5 Å Resolution : resolution of the phase ambiguity by anomalous scattering. Proc. Natl. Acad. Sci. USA, 69, 3185-3188.
313. WATSON, H. C., BRYANT, T. N., WALKER, N. P., SHAW, P. J. & WENDELL, P. L. (1977). The active site of yeast phosphoglycerate kinase. Biochem. Soc. Transactions 5, 652-654.
314. WAWRZYNOW, A., BANECKI, B. & ZYKLICZ, M. (1996). The Clp ATPases define a novel class of molecular chaperones. Molec. Microbiol. 21, 895-899.
315. WEBER, C. H., PARK, Y. S., SANKAR, S., KENT, C. & LUDWIG, M. (1999). A prototypical cytidylyltransferase: CTP: glycerol-3-phosphate cytidlyltransferase from Bacillus subtilis. Structure 7, 1113-1124.
316. WEBER, D. J., BHATNAGAR, S. K., BULLIONS, L. C., BESSMAN, M. J. & MILDVAN, A. S. (1992). NMR and isotope exchange studies of the site of bound cleavage in the MutT reaction. J. Biol. Chem. 267, 16939-16942.
317. WEST, S. C. (1996). DNA Helicases: new breeds of translocating motors and molecular pumps. Cell 86, 177-180.
318. WIERENGA, R. K. & HOL, W. G. J. (1983). Predicted nucleotide-binding properties of p21 protein and its cancer-associated variant. Nature 302, 842-844.
319. WIGLEY, D. B., DAVIES, G. J., DODSON, E. J., MAXWELL, A. & DODSON, G. (1991). Crystal structure of an N-terminal fragment of the DNA gyrase B protein. Nature 351, 624-629.
320. WILBANKS, S. M. & MCKAY, D. B. (1995). How potassium affects the activity of the molecular chaperone Hsc70. J. Biol. Chem. 270, 2251-2257.
321. WILD, K., BOHNER, T., AUBRY, A., FOLKERS, G. & SCHULZ, G. E. (1995). The three-dimensional structure of thymidine kinase from herpes simplex virus type 1. FEBS Lett. 368, 289-292.
322. WILLIAMS, J. C., WEULAND, A., GONFLONI, S., THOMPSON, A., COURTNEIDGE, S. A., SUPERTI-FURGA, G. & WIERENGA, R. K. (1997).The 2.35 Å Crystal structure of the inactivated form of chicken Src: a dynamic molecule with multiple regulatory interactions. J. Mol. Biol. 274, 757-775.
323. WILSON, K. P., FITZGIBBON, M. J., CARON, P. R., GRIFFITH, J. P., CHEN, W., MCCAFFREY, P. G., CHAMBERS, S. P. & SU, M. S. (1996). Crystal structure of p38 mitogen-activated protein kinase. J. Biol. Chem. 271, 27696-27700.
324. WOLODKO, W. T., FRASER, M. E., JAMES, M. N. G. & BRIDGER, W. (1994). The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5-Å resolution. J. Biol. Chem. 269, 10833-10890.
325. XIE, X. L., GU, Y., FOX, T., COLL, J. T., FLEMING, M. A., MARKLAND, W., CARON, P. R., WILSON, K. P. & SU, M. S.-S. (1998). Crystal structure of NJK3: a kinase implicated in neuronal apoptosis. Structure 6, 983-991.
326. XU, R. M., CARMEL, G., SWEET, R. M., KURET, J. & CHENG, X. (1995). Crystal structure of casein kinase-1, a phosphate-directed protein kinase. EMBO J. 14, 1015-1023.
327. XU, W., HARRISON, S. C. & ECK, M. J. (1997). Three-dimensional structure of the tyrosine kinase Src. Nature 385, 595-602.
328. XU, Z., HORWICH, A. L. & SIGLER, P. B. (1997). The crystal structure of the asymmetric GroEL-GroES-(ADP)-chaperonin complex. Nature 388, 741-750.
329. YAMAGUCHI, H. & HENDRICKSON, W. A. (1996). Structural basis for activation of the human lymphocyte kinase Lck upon tyrosine phosphorylation. Nature 384, 484-489.
330. YAMAGUCHI, H., KATO, H., HATA, Y., NISHIOKA, T., KIMURA, A., ODA, J. & KATSUBE, Y. (1993). Three-dimensional structure of the glutatione synthetase from Escherichia coli B at 2.0 Å Resolution. J. Mol. Biol. 229, 1083-1100.
331. YAMASHITA, M. M., ALMASSY, R. J., JANSON, C. A., CASCIO, D. & FISENBERG, D. (1989). Refined atomic-model of glutamine synthetase at 3.5 åangstrom resolution. J. Biol. Chem. 264, 17681-17690.
332. YAN, H., SHI, Z. & TSAI, M.-D. (1990). Mechanism of adenylate kinase. Structural and functional demonstration of arginine-138 as a key catalytic residue that cannot be replaced by lysine. Biochemistry 29, 6385 6392.
333. YAN, S.-Z., HAHN, D., HUANG, Z.-H. & TANG, W.-J. (1996). Two cytoplasmic domains of mammalian adenylyl cyclase form a Gsα- and forskolin-activated enzyme in vitro. J. Biol. Chem. 271, 10941-10945.
334. YANG, W. & STEITZ, T. A. (1995). Crystal structure of the site-specific recombinase gamma-delta resolvase complex with a 34bp cleavage site. Cell 82, 193-207.
335. YAO, N. H., HESSON, T., CABLE, M, HONG, Z., KWONG, A. D., LE, H. V. & WEBER, P. C. (1997). Structure of the hepatitis C virus RNA helicase domain. Nat. Struct. Biol. 4, 463-467.
336. YOSHIDA, M. & AMANO, T. (1995). A common topology of proteins catalyzing ATP-triggered reactions. FEBS Lett. 359, 1-5.
337. YU, R. C., HANSON, P. I., JAHN, R. & BRÜNGER, A. T. (1998). Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP. Nat. Struc. Biol. 5, 803-811.
338. ZAREMBINSKI, T. L., HUNG, L.-W., MUELLER-DIECKMAN, H.-J., KIM, K.-K., YOKOTA, H., KIM, R. & KIM, S.-H. (1998). Structure-based assignment of the biochemical function of a hypothetical protein: A test case of structural genomics. Proc. Natl. Acad. Sci. USA 95, 1518-15193.
339. ZHANG, F., STRAND, A., ROBBINS, D., COBB, M. H. & GOLDSMITH, E. J. (1994). Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution. Nature 367, 704-711.
340. ZHANG, G., LIU, Y., RUOHO, A. E. & HURLEY, J. H. (1997). Structure of the adenylyl cyclase catalytic core. Nature 386, 247-253.
341. ZHANG, P., TOYOSHIMA, C., YONEKURA, K., GREEN, N. K. D. & STOKES, D. L. (1998). Structure of the calcium pump from sarcoplasmic reticulum at 8 Å resolution. Nature 392, 835-839.
342. ZHENG, J., KNIGHTON, D. R., XUONG, N.-H., TAYLOR, S. S., SOWADSKI, J. M. & TEN EYCK, L. F. (1993). Crystal structure of the myristylated catalytic subunit of cAMP-dependent protein kinase reveal open and closed conformation. Protein Science 2, 1559-1573.
343. ZHOU, G., SOMASUNDARAM, T., BLANC, E., PARTHASARATHY, G., ELLINGTON, W. R. & CHAPMAN, M. S. (1998). Transition state structure of arginine kinase: implications for catalysis of bimolecular reactions. Proc. Natl. Acad. Sci. USA 95, 8449-8454.
344. ZHU, X., ZHAO, X., BURKHOLDER, W. F., GRAGEROV, A., OGATA, C. M., GOTTESMAN, M. E. & HENDRICKSON, W. A. (1996). Structural analysis of substrate binding by the molecular chaperone DnaK. Science 272, 1606-1614.