메뉴 건너뛰기




Volumn 369, Issue 1, 2007, Pages 108-128

Crystal Structure of Tryptophanyl-tRNA Synthetase Complexed with Adenosine-5′ Tetraphosphate: Evidence for Distributed Use of Catalytic Binding Energy in Amino Acid Activation by Class I Aminoacyl-tRNA Synthetases

Author keywords

catalytic use of binding energy; class I aminoacyl tRNA synthetases; induced fit; mechanistic enzymology; phosphoryl transfer

Indexed keywords

ADENOSINE; ADENOSINE TETRAPHOSPHATE; ADENOSINE TRIPHOSPHATE; AMINO ACID; AMINO ACID TRANSFER RNA LIGASE; NUCLEOTIDE; PHOSPHATE; TRYPTOPHAN TRANSFER RNA LIGASE; UNCLASSIFIED DRUG;

EID: 34247471258     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.01.091     Document Type: Article
Times cited : (38)

References (79)
  • 1
    • 0029410712 scopus 로고
    • Mapping the transition state for ATP hydrolysis: implications for enzymatic catalysis
    • Admiraal S.J., and Herschlag D. Mapping the transition state for ATP hydrolysis: implications for enzymatic catalysis. Chem. Biol. 2 (1995) 729-739
    • (1995) Chem. Biol. , vol.2 , pp. 729-739
    • Admiraal, S.J.1    Herschlag, D.2
  • 2
    • 33947266906 scopus 로고    scopus 로고
    • A minimal TrpRS catalytic domain supports sense/antisense ancestry of Class I and II aminoacyl-tRNA synthetases
    • Pham Y., Li L., Kim A., Erdogan O., Weinreb V., Butterfosss G., et al. A minimal TrpRS catalytic domain supports sense/antisense ancestry of Class I and II aminoacyl-tRNA synthetases. Mol. Cell 25 (2006) 851-862
    • (2006) Mol. Cell , vol.25 , pp. 851-862
    • Pham, Y.1    Li, L.2    Kim, A.3    Erdogan, O.4    Weinreb, V.5    Butterfosss, G.6
  • 3
    • 0000578929 scopus 로고
    • The effect of bivalent metal ions on the hydrolysis of adenosine di- and tri-phosphates
    • Tetas M., and Lowenstein J.M. The effect of bivalent metal ions on the hydrolysis of adenosine di- and tri-phosphates. Biochemistry 2 (1963) 350-357
    • (1963) Biochemistry , vol.2 , pp. 350-357
    • Tetas, M.1    Lowenstein, J.M.2
  • 4
    • 0030724727 scopus 로고    scopus 로고
    • Mechanisms of signaling and related enzymes
    • Mildvan A.S. Mechanisms of signaling and related enzymes. Proteins: Struct. Funct. Genet. 29 (1997) 401-416
    • (1997) Proteins: Struct. Funct. Genet. , vol.29 , pp. 401-416
    • Mildvan, A.S.1
  • 5
    • 0033102133 scopus 로고    scopus 로고
    • Mechanistic alternatives in phosphate monoester hydrolysis: what conclusions can be drawn from available experimental data?
    • Åqvist J., Kolmodin K., Florian J., and Warshel A. Mechanistic alternatives in phosphate monoester hydrolysis: what conclusions can be drawn from available experimental data?. Chem. Biol. 6 (1999) R71-R80
    • (1999) Chem. Biol. , vol.6
    • Åqvist, J.1    Kolmodin, K.2    Florian, J.3    Warshel, A.4
  • 6
    • 0031646592 scopus 로고    scopus 로고
    • Phosphate ester hydrolysis in aqueous solution: associative versus dissociative mechanisms
    • Florian J., and Warshel A. Phosphate ester hydrolysis in aqueous solution: associative versus dissociative mechanisms. J. Phys. Chem. B 102 (1998) 719-734
    • (1998) J. Phys. Chem. B , vol.102 , pp. 719-734
    • Florian, J.1    Warshel, A.2
  • 7
    • 0012928322 scopus 로고
    • Dissection of the structure and activity of an enzyme
    • Kaiser E.T. (Ed), Robert A. Welch Foundation, Houston, TX
    • Fersht A. Dissection of the structure and activity of an enzyme. In: Kaiser E.T. (Ed). Design of Enzymes and Enzyme Models vol. XXXI (1988), Robert A. Welch Foundation, Houston, TX 159-182
    • (1988) Design of Enzymes and Enzyme Models , vol.XXXI , pp. 159-182
    • Fersht, A.1
  • 8
    • 0023657031 scopus 로고
    • Dissection of the structure and activity of the tyrosyl-tRNA synthetase by site-directed mutagenesis
    • Fersht A.R. Dissection of the structure and activity of the tyrosyl-tRNA synthetase by site-directed mutagenesis. Biochemistry 26 (1987) 8031-8037
    • (1987) Biochemistry , vol.26 , pp. 8031-8037
    • Fersht, A.R.1
  • 9
    • 0026059951 scopus 로고
    • Lysine 335, part of the KMSKS signature sequence, plays a crucial role in the amino acid activation catalyzed by the methionyl-tRNA synthetase from Escherichia coli
    • Mechulam Y., Dardel F., LeCorre D., Blanquet S., and Fayat G. Lysine 335, part of the KMSKS signature sequence, plays a crucial role in the amino acid activation catalyzed by the methionyl-tRNA synthetase from Escherichia coli. J. Mol. Biol. 217 (1991) 465-475
    • (1991) J. Mol. Biol. , vol.217 , pp. 465-475
    • Mechulam, Y.1    Dardel, F.2    LeCorre, D.3    Blanquet, S.4    Fayat, G.5
  • 10
    • 0028883783 scopus 로고
    • Transition state stabilization by the 'high' motif of class I aminoacyl-tRNA synthetases: the case of Escherichia coli methionyl-tRNA synthetase
    • Schmitt E., Panvert M., Blanquet S., and Mechulam Y. Transition state stabilization by the 'high' motif of class I aminoacyl-tRNA synthetases: the case of Escherichia coli methionyl-tRNA synthetase. Nucl. Acids Res. 23 (1995) 4793-4798
    • (1995) Nucl. Acids Res. , vol.23 , pp. 4793-4798
    • Schmitt, E.1    Panvert, M.2    Blanquet, S.3    Mechulam, Y.4
  • 11
    • 0037255536 scopus 로고    scopus 로고
    • Interconversion of ATP binding and conformational free energies by tryptophanyl-tRNA synthetase: structures of ATP bound to open and closed, pre-transition conformations
    • Retailleau P., Huang X., Yin Y., Hu M., Weinreb V., Vachette P., et al. Interconversion of ATP binding and conformational free energies by tryptophanyl-tRNA synthetase: structures of ATP bound to open and closed, pre-transition conformations. J. Mol. Biol. 325 (2003) 39-63
    • (2003) J. Mol. Biol. , vol.325 , pp. 39-63
    • Retailleau, P.1    Huang, X.2    Yin, Y.3    Hu, M.4    Weinreb, V.5    Vachette, P.6
  • 12
    • 0033622155 scopus 로고    scopus 로고
    • 2.9 A crystal structure of ligand-free tryptophanyl-tRNA synthetase: domain movements fragment the adenine nucleotide binding site
    • Ilyin V.A., Temple B., Hu M., Li G., Yin Y., Vachette P., and Carter Jr. C.W. 2.9 A crystal structure of ligand-free tryptophanyl-tRNA synthetase: domain movements fragment the adenine nucleotide binding site. Protein Sci. 9 (2000) 218-231
    • (2000) Protein Sci. , vol.9 , pp. 218-231
    • Ilyin, V.A.1    Temple, B.2    Hu, M.3    Li, G.4    Yin, Y.5    Vachette, P.6    Carter Jr., C.W.7
  • 13
    • 0029643793 scopus 로고
    • Tryptophanyl-tRNA synthetase crystal structure reveals an unexpected homology to tyrosyl-tRNA synthetase
    • Doublie S., Bricogne G., Gilmore C., and Carter Jr. C.W. Tryptophanyl-tRNA synthetase crystal structure reveals an unexpected homology to tyrosyl-tRNA synthetase. Structure 3 (1995) 17-31
    • (1995) Structure , vol.3 , pp. 17-31
    • Doublie, S.1    Bricogne, G.2    Gilmore, C.3    Carter Jr., C.W.4
  • 14
    • 0023122101 scopus 로고
    • Structure of a mutant of tyrosyl-tRNA synthetase with enhanced catalytic properties
    • Brown K.A., Brick P., and Blow D.M. Structure of a mutant of tyrosyl-tRNA synthetase with enhanced catalytic properties. Nature 326 (1987) 416-418
    • (1987) Nature , vol.326 , pp. 416-418
    • Brown, K.A.1    Brick, P.2    Blow, D.M.3
  • 15
    • 14344267196 scopus 로고    scopus 로고
    • High-resolution experimental phases for tryptophanyl-tRNA synthetase (TrpRS) complexed with tryptophanyl-5′AMP
    • Retailleau P., Yin Y., Hu M., Roach J., Bricogne G., Vonrhein C., et al. High-resolution experimental phases for tryptophanyl-tRNA synthetase (TrpRS) complexed with tryptophanyl-5′AMP. Acta Crystallog. sect. D 57 (2001) 1595-1608
    • (2001) Acta Crystallog. sect. D , vol.57 , pp. 1595-1608
    • Retailleau, P.1    Yin, Y.2    Hu, M.3    Roach, J.4    Bricogne, G.5    Vonrhein, C.6
  • 17
    • 0038242280 scopus 로고    scopus 로고
    • Pushing induced fit to its limits: tRNBA-dependent active site assembly in Class I aminoacyl-tRNA synthetases
    • Cavarelli J. Pushing induced fit to its limits: tRNBA-dependent active site assembly in Class I aminoacyl-tRNA synthetases. Structure 11 (2003) 484-486
    • (2003) Structure , vol.11 , pp. 484-486
    • Cavarelli, J.1
  • 18
    • 0034332436 scopus 로고    scopus 로고
    • tRNA aminoacylation by arginyl-tRNA synthetase: induced conformations during substrates binding
    • Delagoutte B., Moras D., and Cavarelli J. tRNA aminoacylation by arginyl-tRNA synthetase: induced conformations during substrates binding. EMBO J. 19 (2000) 5599-5610
    • (2000) EMBO J. , vol.19 , pp. 5599-5610
    • Delagoutte, B.1    Moras, D.2    Cavarelli, J.3
  • 19
    • 0034657687 scopus 로고    scopus 로고
    • The 2 A crystal structure of leucyl-tRNA synthetase and its complex with a leucyl-adenylate analogue
    • Cusack S., Yaremchuk A., and Tukalo M. The 2 A crystal structure of leucyl-tRNA synthetase and its complex with a leucyl-adenylate analogue. EMBO J. 19 (2000) 2351-2361
    • (2000) EMBO J. , vol.19 , pp. 2351-2361
    • Cusack, S.1    Yaremchuk, A.2    Tukalo, M.3
  • 20
    • 0037415750 scopus 로고    scopus 로고
    • ATP Binding by glutamyl-tRNA synthetase is switched to the productive mode by tRNA binding
    • Sekine S.-i., Nureki O., Dubois D.Y., Bernier S., Chênevert R., LaPointe J., et al. ATP Binding by glutamyl-tRNA synthetase is switched to the productive mode by tRNA binding. EMBO J. 22 (2003) 676-688
    • (2003) EMBO J. , vol.22 , pp. 676-688
    • Sekine, S.-i.1    Nureki, O.2    Dubois, D.Y.3    Bernier, S.4    Chênevert, R.5    LaPointe, J.6
  • 22
    • 0016904563 scopus 로고
    • Transition state analog inhibitors and enzyme catalysis
    • Wolfenden R. Transition state analog inhibitors and enzyme catalysis. Annu. Rev. Biophys. Bioeng. 5 (1976) 271-306
    • (1976) Annu. Rev. Biophys. Bioeng. , vol.5 , pp. 271-306
    • Wolfenden, R.1
  • 23
    • 0028916227 scopus 로고
    • Transition state and multisubstrate analog inhibitors
    • Radzicka A., and Wolfenden R. Transition state and multisubstrate analog inhibitors. Methods Enymol. 249 (1995) 284-312
    • (1995) Methods Enymol. , vol.249 , pp. 284-312
    • Radzicka, A.1    Wolfenden, R.2
  • 25
    • 0024332902 scopus 로고
    • Binding of pyrimidine-2one-ribonucleoside by cytidine deaminase as the transition state analogue 3,4-dihydrouridine and the contribution of the 4-hydroxyl group to its binding affinity
    • Frick L., Yang C., Wolfenden R., and Marquez V.E. Binding of pyrimidine-2one-ribonucleoside by cytidine deaminase as the transition state analogue 3,4-dihydrouridine and the contribution of the 4-hydroxyl group to its binding affinity. Biochemistry 28 (1989) 9423-9430
    • (1989) Biochemistry , vol.28 , pp. 9423-9430
    • Frick, L.1    Yang, C.2    Wolfenden, R.3    Marquez, V.E.4
  • 26
    • 0017821705 scopus 로고
    • Control of complex metal ion equilibria in biochemical reaction systems: intrinsic and apparent stability contants of metal adenin nucleotide complexes
    • Adolfson R., and Moudrianakis E. Control of complex metal ion equilibria in biochemical reaction systems: intrinsic and apparent stability contants of metal adenin nucleotide complexes. J. Biol. Chem. 253 (1978) 4378-4379
    • (1978) J. Biol. Chem. , vol.253 , pp. 4378-4379
    • Adolfson, R.1    Moudrianakis, E.2
  • 27
    • 0037306106 scopus 로고    scopus 로고
    • Effects of water soluble phosphotidylserine on bovine factor Xa: functional and structural changes plus dimerization
    • Majumbder R., Wang J., and Lentz B. Effects of water soluble phosphotidylserine on bovine factor Xa: functional and structural changes plus dimerization. Biophys. J. 84 (2003) 1238-1251
    • (2003) Biophys. J. , vol.84 , pp. 1238-1251
    • Majumbder, R.1    Wang, J.2    Lentz, B.3
  • 28
    • 33748454627 scopus 로고    scopus 로고
    • Computational studies of tryptophanyl-tRNA synthetase: activation of ATP by induced-fit
    • Kapustina M., and Carter Jr. C.W. Computational studies of tryptophanyl-tRNA synthetase: activation of ATP by induced-fit. J. Mol. Biol. 362 (2006) 1159-1180
    • (2006) J. Mol. Biol. , vol.362 , pp. 1159-1180
    • Kapustina, M.1    Carter Jr., C.W.2
  • 29
    • 0014931657 scopus 로고
    • An enquiry into the importance of solution effects in phosphate ester and anhydride reactions
    • George P., Witonsky R.J., Trachtman M., Wu X., SoeqER Q., Richman L., et al. An enquiry into the importance of solution effects in phosphate ester and anhydride reactions. Biochim. Biophys. Acta 223 (1970) 1-15
    • (1970) Biochim. Biophys. Acta , vol.223 , pp. 1-15
    • George, P.1    Witonsky, R.J.2    Trachtman, M.3    Wu, X.4    SoeqER, Q.5    Richman, L.6
  • 30
    • 34247543748 scopus 로고    scopus 로고
    • Yin, Y. (1995). Crystallographic study of Bacillus stearothermophilus tryptophanyl-tRNA synthetase in the catalytic reaction. PhD, University of North Carolina at Chapel Hill.
  • 31
    • 0022471120 scopus 로고
    • Use of binding energy in catalysis analyzed by mutagenesis of the tyrosyl-tRNA synthetase
    • Wells T.N.C., and Fersht A.R. Use of binding energy in catalysis analyzed by mutagenesis of the tyrosyl-tRNA synthetase. Biochemistry 25 (1986) 1881-1886
    • (1986) Biochemistry , vol.25 , pp. 1881-1886
    • Wells, T.N.C.1    Fersht, A.R.2
  • 32
    • 0018040470 scopus 로고
    • The assembly of a virus
    • Butler P.J.G., and Klug A. The assembly of a virus. Sci. Am. 239 (1978) 62-69
    • (1978) Sci. Am. , vol.239 , pp. 62-69
    • Butler, P.J.G.1    Klug, A.2
  • 33
    • 0023868490 scopus 로고
    • Reconstruction by site-directed mutagenesis of the transition state for the activation of tyrosine by the tyrosyl-tRNA synthetase: a mobile loop envelopes the transition state in an induced-fit mechanism
    • Fersht A.R., Knill Jones J.W., Bedouelle H., and Winter G. Reconstruction by site-directed mutagenesis of the transition state for the activation of tyrosine by the tyrosyl-tRNA synthetase: a mobile loop envelopes the transition state in an induced-fit mechanism. Biochemistry 27 (1988) 1581-1587
    • (1988) Biochemistry , vol.27 , pp. 1581-1587
    • Fersht, A.R.1    Knill Jones, J.W.2    Bedouelle, H.3    Winter, G.4
  • 34
    • 0029410817 scopus 로고
    • Structure-energy analysis of the role of metal ions in phosphodiester bond hydrolysis by DNA polymerase I
    • Fothergill M., Goodman M., Petruska J., and Warshel A. Structure-energy analysis of the role of metal ions in phosphodiester bond hydrolysis by DNA polymerase I. J. Am. Chem. Soc. 117 (1995) 11619-11627
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 11619-11627
    • Fothergill, M.1    Goodman, M.2    Petruska, J.3    Warshel, A.4
  • 35
    • 0025005059 scopus 로고
    • Free energy relationships in metalloenzyme-catalyzed reactions. Calculations of the effects of metal ion substitutions in staphylococcal nuclease
    • Åqvist J., and Warshel A. Free energy relationships in metalloenzyme-catalyzed reactions. Calculations of the effects of metal ion substitutions in staphylococcal nuclease. J. Am. Chem. Soc. 112 (1990) 2860-2868
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 2860-2868
    • Åqvist, J.1    Warshel, A.2
  • 36
    • 0026019625 scopus 로고
    • Structural basis for the 3′ 5′ exonuclease activity of Escherichia coli DNA polymerase 1: a two metal ion mechanism
    • Beese L.S., and Steitz T.A. Structural basis for the 3′ 5′ exonuclease activity of Escherichia coli DNA polymerase 1: a two metal ion mechanism. EMBO J. 10 (1991) 25-33
    • (1991) EMBO J. , vol.10 , pp. 25-33
    • Beese, L.S.1    Steitz, T.A.2
  • 37
    • 0023707963 scopus 로고
    • Elimination of metals
    • Holmquist B. Elimination of metals. Methods Enymol. 158 (1981) 6-12
    • (1981) Methods Enymol. , vol.158 , pp. 6-12
    • Holmquist, B.1
  • 38
    • 0034684274 scopus 로고    scopus 로고
    • Pentavalent organo-vanadates as transition-state analogues for phosphoryl transfer enzymes
    • Messmore J.M., and Raines R.T. Pentavalent organo-vanadates as transition-state analogues for phosphoryl transfer enzymes. J. Am. Chem. Soc. 122 (2000) 9911-9916
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 9911-9916
    • Messmore, J.M.1    Raines, R.T.2
  • 39
    • 0015497445 scopus 로고
    • Subtilisin: a stereochemical mechanism involving transition state stabilization
    • Robertus J.D., Kraut J., Alden R.A., and Birktoft J.J. Subtilisin: a stereochemical mechanism involving transition state stabilization. Biochemistry 11 (1972) 4293-4303
    • (1972) Biochemistry , vol.11 , pp. 4293-4303
    • Robertus, J.D.1    Kraut, J.2    Alden, R.A.3    Birktoft, J.J.4
  • 40
    • 0029643793 scopus 로고
    • Tryptophanyl-tRNA synthetase crystal structure reveals an unexpected homology to tyrosyl-tRNA synthetase
    • Doublié S., Bricogne G., Gilmore C.J., and Carter Jr. C.W. Tryptophanyl-tRNA synthetase crystal structure reveals an unexpected homology to tyrosyl-tRNA synthetase. Structure 3 (1995) 17-31
    • (1995) Structure , vol.3 , pp. 17-31
    • Doublié, S.1    Bricogne, G.2    Gilmore, C.J.3    Carter Jr., C.W.4
  • 41
    • 14344267196 scopus 로고    scopus 로고
    • High resolution experimental phases for tryptophanyl-tRNA synthetase (TrpRS) complexed with tryptophanyl-5′AMP
    • Retailleau P., Hu M., Bricogne G., Vonrhein C., Roversi P., Blanc E., et al. High resolution experimental phases for tryptophanyl-tRNA synthetase (TrpRS) complexed with tryptophanyl-5′AMP. Acta Crystallog. sect. D 57 (2001) 1595-1608
    • (2001) Acta Crystallog. sect. D , vol.57 , pp. 1595-1608
    • Retailleau, P.1    Hu, M.2    Bricogne, G.3    Vonrhein, C.4    Roversi, P.5    Blanc, E.6
  • 42
    • 0017100947 scopus 로고
    • Theoretical studies of enzymic reactions: dielectric, electrostatic and steric stabilization of the carbonium ion in the reaction of lysozyme
    • Levitt M., and Warshel A. Theoretical studies of enzymic reactions: dielectric, electrostatic and steric stabilization of the carbonium ion in the reaction of lysozyme. J. Mol. Biol. 103 (1976) 227-249
    • (1976) J. Mol. Biol. , vol.103 , pp. 227-249
    • Levitt, M.1    Warshel, A.2
  • 43
    • 0020489430 scopus 로고
    • Conserved cysteine and histidine residues in the structures of the tyrosyl and methionyl-tRNA synthetases
    • Barker D.G., and Winter G. Conserved cysteine and histidine residues in the structures of the tyrosyl and methionyl-tRNA synthetases. FEBS Letters 145 (1982) 191-193
    • (1982) FEBS Letters , vol.145 , pp. 191-193
    • Barker, D.G.1    Winter, G.2
  • 44
    • 0021746195 scopus 로고
    • Specific sequence homology and three-dimensional structure of an aminoacyl transfer RNA synthetase
    • Webster T., Tsai H., Kula M., Mackie G.A., and Schimmel P. Specific sequence homology and three-dimensional structure of an aminoacyl transfer RNA synthetase. Science 226 (1984) 1315-1317
    • (1984) Science , vol.226 , pp. 1315-1317
    • Webster, T.1    Tsai, H.2    Kula, M.3    Mackie, G.A.4    Schimmel, P.5
  • 45
    • 0022443291 scopus 로고
    • Sequence similarities among the family of aminoacyl-tRNA synthetases
    • Hountondji C., Dessen P., and Blanquet S. Sequence similarities among the family of aminoacyl-tRNA synthetases. Biochimie 68 (1986) 1071-1078
    • (1986) Biochimie , vol.68 , pp. 1071-1078
    • Hountondji, C.1    Dessen, P.2    Blanquet, S.3
  • 46
    • 0025158208 scopus 로고
    • Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs
    • Eriani G., Delarue M., Poch O., Gangloff J., and Moras D. Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature 347 (1990) 203-206
    • (1990) Nature , vol.347 , pp. 203-206
    • Eriani, G.1    Delarue, M.2    Poch, O.3    Gangloff, J.4    Moras, D.5
  • 47
    • 0030788568 scopus 로고    scopus 로고
    • The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase
    • Arnez J.G., Augustine J.G., Moras D., and Francklyn C.S. The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase. Proc. Natl Acad. Sci. USA 94 (1997) 7144-7149
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 7144-7149
    • Arnez, J.G.1    Augustine, J.G.2    Moras, D.3    Francklyn, C.S.4
  • 49
    • 0034713835 scopus 로고    scopus 로고
    • Active site of lysyl-tRNA synthetase: structural studies of the adenylation reaction
    • Desogus G., Todone F., Brick P., and Onesti S. Active site of lysyl-tRNA synthetase: structural studies of the adenylation reaction. Biochemistry 39 (2000) 8418-8425
    • (2000) Biochemistry , vol.39 , pp. 8418-8425
    • Desogus, G.1    Todone, F.2    Brick, P.3    Onesti, S.4
  • 50
    • 0027184481 scopus 로고
    • A general two-metal-ion mechanism for catalytic RNA
    • Steitz T.A., and Steitz J.A. A general two-metal-ion mechanism for catalytic RNA. Proc. Natl Acad. Sci. USA 90 (1993) 6498-6502
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6498-6502
    • Steitz, T.A.1    Steitz, J.A.2
  • 51
    • 0027751260 scopus 로고
    • Mutational and kinetic analysis of a mobile loop in tyrosyl-tRNA synthetase
    • First E.A., and Fersht A.R. Mutational and kinetic analysis of a mobile loop in tyrosyl-tRNA synthetase. Biochemistry 32 (1993) 13658-13663
    • (1993) Biochemistry , vol.32 , pp. 13658-13663
    • First, E.A.1    Fersht, A.R.2
  • 53
    • 34247464060 scopus 로고    scopus 로고
    • Tryptophanyl-tRNA synthetases
    • Ibba M., Francklyn C., and Cusack S. (Eds), Landes Biosciences/Eurekah.com, Georgetown, TX
    • Carter Jr. C.W. Tryptophanyl-tRNA synthetases. In: Ibba M., Francklyn C., and Cusack S. (Eds). The Aminoacyl-tRNA Synthetases (2005), Landes Biosciences/Eurekah.com, Georgetown, TX 99-110
    • (2005) The Aminoacyl-tRNA Synthetases , pp. 99-110
    • Carter Jr., C.W.1
  • 54
    • 0028902065 scopus 로고
    • Analysis of the role of the KMSKS loop in the catalytic mechanism of the tyrosyl-tRNA synthetase using multimutant cycles
    • First E.A., and Fersht A.R. Analysis of the role of the KMSKS loop in the catalytic mechanism of the tyrosyl-tRNA synthetase using multimutant cycles. Biochemistry 34 (1995) 5030-5043
    • (1995) Biochemistry , vol.34 , pp. 5030-5043
    • First, E.A.1    Fersht, A.R.2
  • 55
    • 0346103681 scopus 로고    scopus 로고
    • Crystal structures that suggest late development of genetic code components for differentiating aromatic side chains
    • Yang X.-L., Otero F.J., Skene R.J., McRee D.E., Schimmel P., and Ribas de Pouplana L.s. Crystal structures that suggest late development of genetic code components for differentiating aromatic side chains. Proc. Natl Acad. Sci. USA 100 (2003) 15376-15380
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 15376-15380
    • Yang, X.-L.1    Otero, F.J.2    Skene, R.J.3    McRee, D.E.4    Schimmel, P.5    Ribas de Pouplana, L.s.6
  • 56
    • 0035814899 scopus 로고    scopus 로고
    • Characterization of the transition-state structure of the reaction of kanamycin nucleotydyltransferase by heavy-atom kinetic isotope effects
    • Gerretana B., Frey P.A., and Cleland W.W. Characterization of the transition-state structure of the reaction of kanamycin nucleotydyltransferase by heavy-atom kinetic isotope effects. Biochemistry 40 (2001) 2972-2977
    • (2001) Biochemistry , vol.40 , pp. 2972-2977
    • Gerretana, B.1    Frey, P.A.2    Cleland, W.W.3
  • 57
    • 0032860328 scopus 로고    scopus 로고
    • Enzymatic transition-state analysis and transition-state analogs
    • Schramm V.L. Enzymatic transition-state analysis and transition-state analogs. Methods Enzymol. 308 (1999) 301-355
    • (1999) Methods Enzymol. , vol.308 , pp. 301-355
    • Schramm, V.L.1
  • 58
    • 84961974064 scopus 로고    scopus 로고
    • Computer simulation of the chemical catalysis of DNA polymerases: discriminating between alternative nucleotide insertion mechanisms for T7 DNA polymerase
    • Florian J., Goodman M., and Warshel A. Computer simulation of the chemical catalysis of DNA polymerases: discriminating between alternative nucleotide insertion mechanisms for T7 DNA polymerase. J. Am. Chem. Soc. 125 (2003) 8163-8177
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 8163-8177
    • Florian, J.1    Goodman, M.2    Warshel, A.3
  • 59
    • 18744402486 scopus 로고    scopus 로고
    • Computer simulations of protein functions: searching for the molecular origin of the replication fidelity of DNA polymerases
    • Florian J., Goodman M., and Warshel A. Computer simulations of protein functions: searching for the molecular origin of the replication fidelity of DNA polymerases. Proc. Natl Acad. Sci. 102 (2005) 6819-6824
    • (2005) Proc. Natl Acad. Sci. , vol.102 , pp. 6819-6824
    • Florian, J.1    Goodman, M.2    Warshel, A.3
  • 60
    • 0019153831 scopus 로고
    • Rapid separation of nucleoside mono-,di-, and triphosphates on ion-exlcusion/exchange columns
    • Leigh C.P.H., and Cashion P.J. Rapid separation of nucleoside mono-,di-, and triphosphates on ion-exlcusion/exchange columns. J. Chromatog. 192 (1980) 490-493
    • (1980) J. Chromatog. , vol.192 , pp. 490-493
    • Leigh, C.P.H.1    Cashion, P.J.2
  • 61
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinoski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinoski, Z.1    Minor, W.2
  • 62
    • 0000952473 scopus 로고
    • On the treatment of negative intensity observations
    • French G.S., and Wilson K.S. On the treatment of negative intensity observations. Acta Crystallog. sect. A 34 (1978) 517-525
    • (1978) Acta Crystallog. sect. A , vol.34 , pp. 517-525
    • French, G.S.1    Wilson, K.S.2
  • 63
    • 0028103275 scopus 로고
    • The CCP4 Suite: a programs for protein crystallography
    • CCP4. The CCP4 Suite: a programs for protein crystallography. Acta Crystallog. sect. D 50 (1994) 760-76364
    • (1994) Acta Crystallog. sect. D , vol.50 , pp. 760-76364
    • CCP41
  • 64
    • 0026817874 scopus 로고
    • Identification of heavy-atom derivatives by normal probability methods
    • Howell L., and Smith D. Identification of heavy-atom derivatives by normal probability methods. J. Appl. Crystallog. 25 (1992) 81-86
    • (1992) J. Appl. Crystallog. , vol.25 , pp. 81-86
    • Howell, L.1    Smith, D.2
  • 65
    • 0031053055 scopus 로고    scopus 로고
    • AMoRe: an automated molecular replacement package
    • Navaza J. AMoRe: an automated molecular replacement package. Methods Enymol. 276 (1997) 581-594
    • (1997) Methods Enymol. , vol.276 , pp. 581-594
    • Navaza, J.1
  • 67
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • de La Fortelle E., and Bricogne G. Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276 (1997) 472-494
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • de La Fortelle, E.1    Bricogne, G.2
  • 69
    • 0347383760 scopus 로고    scopus 로고
    • ARP/wARP and automatic interpretation of protein electron density maps
    • Myers R.J., Perrakis A., and Lamzin V.S. ARP/wARP and automatic interpretation of protein electron density maps. Methods Enymol. 374 (2003) 229-244
    • (2003) Methods Enymol. , vol.374 , pp. 229-244
    • Myers, R.J.1    Perrakis, A.2    Lamzin, V.S.3
  • 70
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallog. sect. D 53 (1997) 240-255
    • (1997) Acta Crystallog. sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.2    Dodson, E.J.3
  • 71
    • 0031059040 scopus 로고    scopus 로고
    • Bayesian statistical viewpoint on structure determination: basic concepts and examples
    • Bricogne G. Bayesian statistical viewpoint on structure determination: basic concepts and examples. Methods Enzymol. 276 (1997) 361-423
    • (1997) Methods Enzymol. , vol.276 , pp. 361-423
    • Bricogne, G.1
  • 73
    • 0030757720 scopus 로고    scopus 로고
    • TNT refinement package
    • Tronrud D.E. TNT refinement package. Methods Enzymol. 277 (1997) 306-319
    • (1997) Methods Enzymol. , vol.277 , pp. 306-319
    • Tronrud, D.E.1
  • 74
    • 0030498233 scopus 로고    scopus 로고
    • Efficient rebuilding of protein structures
    • Kleywegt G.A., and Jones T.A. Efficient rebuilding of protein structures. Acta Crystallog. sect. D 52 (1996) 826-828
    • (1996) Acta Crystallog. sect. D , vol.52 , pp. 826-828
    • Kleywegt, G.A.1    Jones, T.A.2
  • 75
    • 0032922193 scopus 로고    scopus 로고
    • SFCHECK: a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model
    • Vaguine A.A., Richelle J., and Wodak S.J. SFCHECK: a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model. Acta Crystallog. sect. D 55 (1999) 191-205
    • (1999) Acta Crystallog. sect. D , vol.55 , pp. 191-205
    • Vaguine, A.A.1    Richelle, J.2    Wodak, S.J.3
  • 76
    • 0027169515 scopus 로고
    • Main-chain bond lengths and bond angles in protein structures
    • Laskowski R.A., Moss D.S., and Thornton J.M. Main-chain bond lengths and bond angles in protein structures. J. Mol. Biol. 231 (1993) 1049-1067
    • (1993) J. Mol. Biol. , vol.231 , pp. 1049-1067
    • Laskowski, R.A.1    Moss, D.S.2    Thornton, J.M.3
  • 77
    • 0026244229 scopus 로고
    • MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
    • Kraulis P. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24 (1991) 946-950
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 78
    • 0028057108 scopus 로고
    • Raster 3D version 2.0: a program for photorealistic molecular graphics
    • Merrit E.A., and Murphy M.E.P. Raster 3D version 2.0: a program for photorealistic molecular graphics. Acta Crystallog. sect. D 50 (1994) 869-873
    • (1994) Acta Crystallog. sect. D , vol.50 , pp. 869-873
    • Merrit, E.A.1    Murphy, M.E.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.