Mechanisms of cooperativity and allosteric regulation in proteins

Quarterly Reviews of Biophysics

Volumn 22, Issue 2, 1989, Pages 139-237

  Perutz, M F ^a  

^a MRC LABORATORY OF MOLECULAR BIOLOGY   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

HEMERYTHRIN; HEMOCYANIN; HEMOGLOBIN;

ALLOSTERISM; GLYCOLYSIS; PRIORITY JOURNAL; REVIEW;

ALLOSTERIC REGULATION; BINDING SITES; BIOPHYSICS; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEINS; SUPPORT, NON-U.S. GOV'T; SUPPORT, U.S. GOV'T, NON-P.H.S.; SUPPORT, U.S. GOV'T, P.H.S.;

EID: 0024953088     PISSN: 00335835     EISSN: 14698994     Source Type: Journal    
DOI: 10.1017/S0033583500003826     Document Type: Article

References (164)

1. Abelson, P. H., (1954). Amino acid biosynthesis in Escherichia coli: Isotopic competition with l4C glucose, J. biol. Chem. 206, 335-343.
2. 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.
3. Amit, A. G., Mariuzza, R. A., Phillips, S.E.V. & Poljak, R.J. (1986). Three dimensional structure of an antigen-antibody complex at 2-8 A resolution. Science 233. 747-753.
4. Antonini, E. & Brunori, M. (1971). Hemoglobin and Myoglobin and their Reactions with Oxygen, pp. 241, 394. Amsterdam: North Holland.
5. Angel, W.-L., Karplus, M., Poyart, C. & Burseaux, E. (1988). Analysis of proton release in oxygen binding by haemoglobin: Implications for the cooperative mechanism. Biochemistry 27, 1285-1301.
6. Armstrong, W.H. & Lippard, S.J. (1984). Reversible protonation of the oxo bridge in a haemerythrin model compound. J. Am. Chem. Soc. 106, 4632-4633.
7. Armstrong, W. H., Spool, A., Papaefthymiou, G. C., Frankel, R.B. & Lippard, S.J. (1984). Assembly and characterisation of an accurate model for the diiron center in hemerythrin. J. Am. Chem. Soc. 106, 3653-3667.
8. Arnone, A. (1972). X-ray diffraction study of binding of 2,3-diphosphoglycerate to human deoxyhaemoglobin. Nature 237, 146-149.
9. Arrowsmith, C. H., Carey, J., Treat-Clemons, L. & Jardetzky, O. (1989). NMR assignments for the amino-terminal residues of trp repressor and their role in DNA binding. Biochemistry 28, 3875-3885.
10. Baldwin, J.M. (1975). Structure and function of haemoglobin. Progr. Biophys. molec. Biol. 29, 225-320.
11. Baldwin, J.M. & Chothia, C. (1979). Haemoglobin: The structural changes related to ligand binding and its allosteric mechanism. J. molec. Biol. 129, 183-191.
12. Barford, D. & Johnson, L.N. (1989). The allosteric transition of glycogen phosphorylase. Nature (in the Press).
13. Bass, S., Sugiono, P., Arvidson, D. N., Gunsalus, R.P. & Youderian, P. (1987). RNA specificity determinants of E. coli tryptophan repressor binding. Genes & Development I., 565-572.
14. Bennett, W.S. & Steitz, T.A. (1978). Glucose-induced conformational change in yeast hexokinase. Proc. natn. Acad. Sci. U.S.A. 75, 4848-4852.
15. Berger, S.A. & Evans, P.R. (1989). Active site mutants altering the cooperativity of E. coli phosphofructokinase. (In preparation.)
16. Blackburn, M.N. & Schachman, H.K. (1977). Allosteric regulation of aspartate transcarbamylase. Effect of active site ligands on the reactivity of sulfydryl groups of the regulatory subunits. Biochemistry 16, 5084-5090.
17. Blangy, D., Buc, H. & Monod, J. (1968). Kinetics of the allosteric interactions of phosphofructokinase from Escherichia coli. J. molec. Biol. 31, 13-35.
18. Bloomer, A.C. & Butler, P.J.G. (1986). Tobacco mosaic virus: Structure and assembly. In The Plant Viruses (ed. M.B.V. van Regenmortel and H. Fraenkel Conrat). Plenum.
19. Bloomer, A. C., Champness, J. N., Bricogne, G., Staden, R. & Klug, A. (1978). Protein disk of tobacco mosaic virus at 2-8 A resolution showing interactions within and between the subunits. Nature 276, 362-368.
20. Bolognesi, M., Cannillo, E., Ascenzi, P., Giacometti, G. M., Merli, A. & Brunori, M. (1982). Reactivity of ferric Aplysia and sperm whale myoglobins towards imidazole: X-ray and binding study. J. molec. Biol. 158, 305-315.
21. Bonaventura, C., Sullivan, B., Bonaventura, J. & Bourne, S. (1974). CO binding by hemocyanins of Limulus polyphemus, Busycon carica and Callinectes sapidus. Bio chemistry 13, 4784-4789.
22. Briehl, R.W. (1963). The relation between the oxygen equilibrium and aggregation of subunits in lamprey hemoglobin. J. biol. Chem. 238, 2361-2366.
23. Brown, J. M., Powers; L., Kinkaid, B., Larrobee, J.A. & Spiro, T.G. (1980). Hemocyanin active site characterization and resonance Raman spectroscopy. J. Am. Chem. Soc. 102, 4210-4216.
24. Brunori, M., Kuiper, H.A. & Zolla, L. (1982). Ligand binding and stereochemical effects in hemocyanins. EMBO J. 1, 329-331.
25. Bunn, H.F. & Forget, G.B. (1985). Hemoglobin, Molecular and Clinical Aspects. Philadelphia: W.B. Saunders.
26. Butler, P.J.G. & Durham, A.C.H. (1977). Tobacco mosaic virus protein aggregation and the virus assembly. Adv. Prot. Chem. 31, 187-251.
27. Butler, P.J.G. & Klug, A. (1978). The assembly of a virus. Sci. Am. 239, 52-59.
28. Calhoun, D. B., Vanderkooi, J. M., Woodrow, G.V. III & Englander, S.W. (1983). Penetration of dioxygen into proteins studied by quenching of phos phorescence and fluorescence. Biochemistry 22, 1526-1532.
29. Carey, J. (1988). Gel retardation at low pH resolves trp repressor-DNA complexes for quantitative study. Proc. natn. Acad. Sci. U.S.A. 85, 975-979.
30. Carey, J. (1989). trp Repressor arms contribute binding energy without occupying unique locations on DNA.J. biol. Chem. 264, 1941-1945.
31. Carmichael, V. E., Dutton, P. J., Fyles, T. M., James, T. D., Swan, J.A. & Zojaji, M. (1989). Biomimetic ion transport: A functional model of a unimolecular ion channel. J. Am. Chem. Soc. i n., 767-769.
32. Caspar, D. (1963). Assembly and stability of the tobacco mosaic virus particle. Adv. Prot. Chem. 18, 37-121.
33. Cash, D.J. & Hess, G.P. (1980). Molecular mechanism of acetylcholine-controlled ion translocation across cell membranes. Proc. natn. Acad. Sci. U.S.A. 77, 842-846.
34. Changeux, J.P. (1961). The feedback mechanism of biosynthetic L-threonine deaminase by L-isoleucine. Cold Spring Harb. Symp. quant. Biol. 26, 313-318.
35. Changeux, J. P., Gerhardt, J.C. & Schachman, H.K. (1968). Allosteric interaction in aspartate transcarbamylase. 1. Binding of specific ligands to the native enzyme and its isolated subunits. Biochemistry 7, 531-538.
36. Changeux, J. P., Giraudat, J. & Dennis, M. (1987). The nicotinic acid acetylcholine receptor: Molecular architecture of a ligand-regulated ion channel. Trends pharmac. Sci. 8, 450-465.
37. Changeux, J.P. & Rubin, M.M. (1968). Allosteric interactions in aspartate trans carbamylase. III. Interpretation of experimental data in terms of the model of Monod, Wyman & Changeux. Biochemistry 7, 553-560.
38. Cheng, X. & Schoenborn (1989). Private communication.
39. Chothia, C. & Lesk, A.M. (1985). Helix movements in proteins. Trends in Biochem. Sci. 10, 116-118.
40. Chu, A. H., Turner, B.W. & Ackers, G.K. (1984). Effects of protons on the oxygen linked subassembly in human hemoglobin. Biochemistry 23, 604-617.
41. Cohen, G. & Jacob, F. (1959). Sur la repression de la synthese des enzymes intervenants dans la formation du tryptophane chez Escherichia coli. C.R. Hebd. se'anc. Acad. Sci., Paris 248, 3490-3492.
42. Connelly, P. R., Gill, S. J., Miller, K. I., Zhou, G. & Van Holde, K.E. (1989). Identical linkage and cooperativity of oxygen and carbon monoxide binding to Octopus dofleini hemocyanin. Biochemistry 28, 1835-1843.
43. Crick, F.H.C. & Orgel, L.E. (1964). The theory of interallelic complementation. J. molec. Biol. 8, 161-165.
44. Crothers, D.M. & Metzger, H. (1972). The influence of polyvalency on the binding properties of antibodies. Immunochemistry 9, 341-357.
45. Dalvit, C. & Wright, P.E. (1987). Assignment of resonances in the *H nuclear magnetic resonance spectrum of the carbonmonoxide complex of sperm whale myoglobin by phase-sensitive two-dimensional techniques. J. molec. Biol. 194, 313-327.
46. Derewenda, Z., Dodson, G., Emsley, P., Harris, D., Nagai, K., Perutz, M.F. & Renaud, J.-P. (1989). The stereochemistry of CO binding to normal human adult and Cowtown hemoglobins. J. molec. Biol. (in the Press).
47. Dickerson, R.E. & Geis, I. (1983). Haemoglobin: Structure, Function, Evolution, Pathology. Kenlo Park: Benjamin/Cummings.
48. Eisenberg, D., Almassy, R. J., Janson, C.A. Chapman, M. S., Shuh, S. W., Cascio, D. & Smith, W.W. (1987). Some evolutionary relationships of the primary biological catalysts glutamine synthetase and RuBisCo. Cold Spring Harb. Symp. quant. Biol. 52, 483-490.
49. Eisenstein, E., Markby, D.W. & Schachman, H.K. (1989). Changes in stability and allosteric properties of aspartate transcarbamyolase resulting from amino acid substitutions in the zinc-binding domain of the regulatory chains. Proc. natn. Acad. Sci. U.S.A. 86, 3094-3098.
50. Elam, W. T., Stern, E. A., Mccallum, J.D. & Sanders-Loehr, J. (1983). An X-ray absorption study of the binuclear iron center in deoxyhemerythrin. J. Am. Chem. Soc. 105, 1919-1923.
51. Elber, R. & Karplus, M. (1989). Molecular dynamics simulations of myoglobin. (To be published.)
52. Ellerton, H. D., Ellerton, N.F. & Robinson, H.A. (1983). Hemocyanin-a current perspective. Progr. Biophys. Molec. Biol. 41, 143-248.
53. Englander, S.W. & Kallenbach, N.R. (1984). Hydrogen exchange and structural dynamics of proteins and nucleic acids. Q. Rev. Biophys. 16, 521-565.
54. Evans, D. R., Styliani, C.P.-L. & Lipscomb, W.N. (1975). Isolation and properties of a species produced by the partial dissociation of aspartate transcarbamylase from Escherichia coli.J. biol. Chem. 250 (10), 3571-3583.
55. Evans, P.R. & Hudson, P.J. (1979). Structure and control of phosphofructokinase from Bacillus stearothermophilus. Nature 279, 500-504.
56. Evans, P. R., Farrants, G.W. & Lawrence, M.C. (1986). Crystallographic structure of allosterically inhibited phosphofructokinase at 7 A resolution. J. molec. Biol. 191, 713-720.
57. Fermi, G. & Perutz, M.F. (1981). Atlas of Molecular Structures in Biology: Haemoglobin & Myoglobin. Oxford: Clarendon Press.
58. Fersht, A. R., Leatherbarrow, R.J. & Wells, T.N.C. (1986). Structure and activity of the tyrosyl-tRNA synthetase: The hydrogen bond in catalysis and specificity. Phil. Trans. R. Soc. Lond. A317, 305-320.
59. Fincham, J.R.S. & Day, P.R. (1963). Fungal Genetics. Oxford: Blackwell Scientific Publications.
60. Fletterick, R.J. & Madsen, N.B. (1980). The structures and related functions of phosphorylase a.A. Rev. Biochem. 49, 31-61.
61. Fletterick, R.J. & Sprang, S.R. (1982). Glycogen phosphorylase structures and function. Ace. Chem. Res. 15, 361-369.
62. Foote, J. & Schachman, H.K. (1985). Homotropic effects in aspartate trans carbamylase: What happens when the enzyme binds a single molecule of the bisubstrate analogue iV-phosphonacetyl-L-aspartate? J. molec. Biol 186, 175-184.
63. Frederick, C. A., Grable, J., Melia, M., Samudzi, C., Jen-Jacobson, L., Wang, B. C., Greene, P., Boyer, H.W. & Rosenberg, J.M. (1984). Kinked DNA in crystalline complex with Eco Ri endonuclease. Nature 309, 327-331.
64. Frey, J. G., Eisenberg, D. & Eiserling, F.A. (1975). Glutamine synthetase forms three-and seven-stranded cables. Proc. natn. Acad. Sci. U.S.A. 72, 3402-3406.
65. Gaykema, W.P.J., Hol, W.G.J., Vereijken, J. M., Soeter, N. M., Bak, H.J. & Beintema, J.J. (1984). 3 2 A structure of the copper-containing, oxygen-carrying protein Panulirus interruptus haemocyanin. Nature 309, 23-29.
66. Gelin, R. G., Lee, A.W.-M. & Karplus, M. (1983). Hemoglobin tertiary structural change on ligand binding. Its role in the cooperative mechanism. J. molec. Biol. 171, 480-559.
67. Gerhardt, J.C. & Pardee, A.B. (1962). The enzymology of control by feedback inhibition. J. biol. Chem. 237, 891-896.
68. Gerhardt, J.C. & Schachman, H.K. (1968). Allosteric interactions in aspartate transcarbamylase II. Evidence for different conformational states of the protein in the presence and absence of specific ligands. Biochemistry 7, 538-552.
69. Gibbons, I., Ritchey, J.M. & Schachman, H.K. (1976). Concerted allosteric transitions in hybrids of aspartate transcarbamylase containing different arrangements of active and inactive sites. Biochemistry 15, 1324-1330.
70. Gibbons, I., Yang, Y.R. & Schachman, H.K. (1974). Cooperative interactions in aspartate transcarbamylase. I. Hybrids composed of native and chemically inactivated catalytic chains. Proc. natn. Acad. Sci. U.S.A. 71, 4452-4456.
71. Gill, S. J., Di Cera, E., Doyle, M.L. & Robert, C.H. (1988). New twists on an old story: Hemoglobin. Trends biochem. Sci. 13, 465-467.
72. Giraudat, J., Dennis, M., Heitmann, T., Haumont, P. T., Lederer, F. & Changeux, J.P. (1987). Structure of the high-affinity binding sites for non-competitive blockers of the acetylcholine receptor: [3H]chlorpromazine labels homologous residues in the P and S chains. Biochemistry 26, 2410-2418.
73. Goldsmith, E., Sprang, S. & Fletterick, R.J. (1982). Structure of maltoheptaose by difference Fourier methods and a model for glycogen. J. molec. Biol. 156, 411-423.
74. Goldsmith, E. J., Sprang, S. R., Hamlin, R., Xuong, N. & Fletterick, R.J. (1989). Domain separation in the activation of glycogen phosphorylase a. (Submitted to Science.)
75. Gopalakrishnan, P.V. & Karush, F. (1974). Antibody affinity. VII. Multivalent interaction of anti-lactoside antibody. J. Immunol. 113, 769-778.
76. Graves, D.J. & Wang, J.H. (1972). a-glucan phosphorylases-chemical and physical basis of catalysis and regulation. In The Enzymes, (ed. P.D. Boyer) vol. 7, PP. 435-482. New York: Academic Press.
77. Gunsalus, R. P., Gunsalus, M.A. & Gunsalus, G.L. (1986). Intracellular trp repressor levels in Escherichia coli. J. Bacteriol. 167, 272-278.
78. Hajdu, J., Acharya, K. R., Stuart, D. I., Mclaughlin, P. J., Barford, D., Oikonomakos, N. G., Klein, H. & Johnson, L.N. (1987). Catalysis in the crystal: Synchrotron radiation studies with glycogen phosphorylase b. EMBO jf. 6, 539-545.
79. Heidmann, T., Beuchardt, J. Neumann, E. & Changeux, J.P. (1983). Rapid kinetics of agonist binding and permeability response analysed in parallel on acetylcholine receptor-rich membranes from Torpedo marmorata. Biochemistry 22, 5452-5459.
80. Heidner, E. J., Frey, T.G. Held, J., Weissman, L. J., Fenna, R. E., Lei, M., Harel, M., Kabsch, H., Sweet, R.M. & Eisenberg, D. (1978). New crystal forms of glutamine synthetase and implications for the molecular structure. J. molec. Biol. 122, 163-173.
81. Hellinga, H.W. & Evans, P.R. (1987). Mutations in the active site of Escherichia coli phosphofructokinase. Nature 327, 437-439.
82. Helmreich, E.J.M. & Klein, H.W. (1980). The role of pyridoxal phosphate in the catalysis of glycogen phosphorylase. Angew. Chem. Int. Ed. Eng. 19, 441-455.
83. Hendrickson, W.A. & Love, W.E. (1971). Structure of lamprey haemoglobin. Nature New Biol. 232, 197-203.
84. Herve, J. (1989). Aspartate transcarbamylase from E. coli. In Allosteric Enzymes (ed. G. Herve) CRC Press (in the Press).
85. Herve, G., Moody, M. F., Tave, P., Vachette, P. & Jones, P.T. (1985). Quaternary structure changes in aspartate transcarbamylase by X-ray scattering. J. molec. Biol. 185, 189-199.
86. Honzatko, R. B., Crawford, J. L., Monaco, H. L., 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 structure of native and CTP-liganded aspartate carbamoyltransferase from Escherichia coli. J. molec. Biol. 160, 219-263.
87. Honzatko, R.B. & Lipscomb, W.N. (1982). Interactions of phosphate ligands with Escherichia coli aspartate carbamoyltransferase in the crystalline state, jf. molec. Biol. 160, 265-286.
88. Howlett, G. J., Blackburn, M. N., Compton, J.G. & Schachman, H.K. (1977). Allosteric regulation of aspartate transcarbamylase. Analysis of the structural and functional behaviour in terms of a two-state model. Biochemistry 16, 5091-5099.
89. Howlett, G.J. & Schachman, H.K. (1977). Allosteric regulation of aspartate transcarbamylase. Changes in the sedimentation coefficient promoted by the bisubstrate analogue JV-(phosphonacetyl)-L-aspartate. Biochemistry 16, 5077-5083.
90. Imai, K., (1982). Allosteric Effects in Haemoglobin. Cambridge University Press.
91. Jarvest, R. L., Lowe, G. & Potter, B.V.L. (1981). The stereochemical course of phosphoryl transfer catalyzed by Bacillus stearothermophilus and rabbit-muscle phosphofructokinase with a chiral [160, 170, 180,] phosphate ester. Biochem. J. 199, 427-432.
92. Joachimiak, A. J., Kelley, R. L., Gunsalus, R. P., Yanofsky, C. & Sigler, P.B. (1983). Purification and characterization of the trp aporepressor. Proc. natn. Acad. Sci. U.S.A. 80, 668-672.
93. Johnson, B. A., Bonaventura, C. & Bonaventura, J. (1984). Allosteric modulation of Callinectes sapidus haemocyanin by lactate. Biochemistry 23, 872-878.
94. Johnson, K. A., Olson, J.S. & Phillips, G.N. Jr. (1989). The structure of myoglobin ethyl isocyanide: Histidine as a swinging door for ligand entry. J. molec. Biol. 207, 459-463.
95. Johnson, L. N., Hajdu, J., Acharya, K. R., Stuart, D. I., Mclaughlin, P. J., Oikonomakos, N.G. & Barford, D. (1989). Glycogen phosphorylase b. In Allosteric Proteins (ed. G. Herve), CRC Press.
96. Jullien, L. & Lehn, J.-M. (1988). The “Chundle” approach to molecular channels: Synthesis of a macrocycle-based molecular bundle. Tetrahedron Lett. 29 (31), 3803-3806.
97. Kantrowitz, E.R. & Lipscomb, W.N. (1988). Escherichia coli aspartate trans carbamylase: The relations between structure and function. Science 241, 669-674.
98. Karush, F. (1978). The affinity of antibody: Range, variability, and the role of multivalence. In Immunoglubulins (ed. G.W. Littman and R.A. Good), pp. 85-115.
99. Ke, H.-M., Honzatko, R.B. & Lipscomb, W. N., (1984). Structure of unligated aspartate carbamoyltransferase of Escherichia coli at 2-6 A resolution. Proc. natn. Acad. Sci. U.S.A. 81, 4037-4040.
100. Ke, H., Lipscomb, W. N., Cho, Y. & Honzatko, R.B. (1988). Complex of N phosphonyl-L-aspartate with aspartate carbamoyltransferase. X-ray refinement, analysis of conformational changes and catalytic and allosteric mechanisms. J. molec. Biol. 204, 725-747.
101. Kelly, R. & Yanofsky, C. (1985). Mutational studies with the trp repressor of E. coli support the helix-turn-helix model of repressor recognition of operator DNA. Proc. natn. Acad. Set. U.S.A. 82, 483-487.
102. Kilmartin, J.V. (1974). Influence of DPG on the Bohr effect of human haemoglobin. FEBS Lett. 38, 147-148.
103. Kilmartin, J. V., Breen, J. J., Roberts, G.C.K. & Ho, C. (1973). Direct measurement of the pK values of an alkaline Bohr group in human haemoglobin. Proc. natn. Acad. Sci. U.S.A. 70, 1246-1249.
104. Kim, K., Fettinger, J., Sessler, J. L., Cyr, M., Hugdahl, J., Collman, J.P. & Ibers, J.A. (1989). Structural characterisation of a sterically encumbered iron(n) porphyrin CO complex. J. Am. Chem. Soc. 111, 403-405.
105. Klug, A. & Rhodes, D. (1987). ‘Zinc finger's: A novel protein motif for nucleic acid recognition. Trends biochem. Sci. 12, 464-469.
106. Knowles, J. (1980). Enzyme-catalyzed phosphoryl transfer reactions. An. Rev. Biochem. 49. 877-918.
107. Koshland, D.E. (1959). In The Enzymes, 2nd ed. vol. 1 (ed. P.D. Boyer, H. Lardy & K. Myrback), pp. 305-346. New York: Academic Press.
108. Koshland, D. E., Nemethy, G. & Filmer, D. (1966). Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochemistry 5, 365-385.
109. Kotlarz, D. & Buc, H. (1982). Phosphofructokinases from Escherichia coli. Methods Enzymol. 90, 60-70.
110. Krause, K. L., Volz, K.W. & Lipscomb, W.N. (1987). 2-5 A structure of aspartate carbamoyltransferase complexed with the bisubstrate analog iV-(phosphonacetyl)-Laspartate. J. molec. Biol. 193, 527-553.
111. Krebs, E.G. (1986). The enzymology of control by phosphorylation. In The Enzymes, 3rd ed. vol. 17 (ed. P.D. Boyer and E.G. Krebs), pp. 3-20. New York: Academic Press.
112. Krose, J., Kruse, K. M., Witz, J., Chauvin, C., Jacrot, B. & Tardieu, A. (1982). Divalent ion-dependent reversible swelling of tomato bushy stunt virus and organisation of the expanded virion. J. molec. Biol. 162, 393-417.
113. Kuiper, H., Antonini, E. & Brunori, M. (1977). Kinetic control of cooperativity in the oxygen binding of Panulirus interruptus haemocyanin. jf. molec. Biol. 116, 569-576.
114. Kuiper, H., Forlani, L., Chiancone, E., Antonini, E., Brunori, M. & Wyman, J. (1979). Multiple linkage in Panulirus interruptus. Biochemistry 18, 5849-5854.
115. Kuiper, H., Gaastra, W., Beintema, J. J., Van Bruggen, E.F.J., Schepman, A.M.H. & Drenth, J. (1975). Subunit composition, X-ray diffraction, amino acid analysis and oxygen binding behaviour of Panulirus interruptus hemocyanin. J. molec. Biol. 99, 619-629.
116. Kuriyan, J., Wilz, S., Karplus, M. & Petsko, G.A. (1986). X-ray structure and refinement of carbonmonoxy (Fell)-myoglobin at 1-5 A resolution. J. molec. Biol. 192, 133-154.
117. Ladjimi, M.M. & Kantrowitz, E.R. (1988). A possible model for the concerted transition in Escherichia coli aspartate transcarbamylase as deduced from site-directed mutagenesis studies. Biochemistry 27, 276-283.
118. Ladjimi, M. M., Middleton, S. A., Kellerher, K.S. & Kantrowitz, E.R. (1988). Relationship between domain closure and binding, catalysis and regulation in Escherichia coli aspartate transcarbamylase. Biochemistry 27, 268-276.
119. Lakowicz, J.R. & Weber, G. (1973). Quenching of protein fluorescence by oxygen. Detection of structural fluctuations in proteins on the nanosecond time scale. Biochemistry 12, 4171-4179.
120. Lalezari, I., Rahbar, S., Lalezari, P., Fermi.G. & Perutz, M.F. (1988). LR16, a compound with potent effects on the oxygen affinity of hemoglobin, on blood cholesterol, and on low density lipoprotein. Proc. natn. Acad. Sci. U.S.A. 85, 6117-6121.
121. Lamy, J., Leclerc, M., Sizaret, P.-Y., Lamy, J., Miller, K. I., Mcparland, R. & Van Holde, K.E. (1987). Octopus dofleini hemocyanin: Structure of the seven-domain polypeptide chain. Biochemistry 26, 3509-3518.
122. Lau, F.T.-K. & Fersht, A.R. (1987). Conversion of allosteric inhibition to activation in phosphofructokinase by protein engineering. Nature 326, 811-812.
123. Lau, F.T.-K., Fersht, A. R., Hellinga, H.W. & Evans, P.R. (1987). Site-directed mutagenesis in the effector site of Escherichia coli phosphofructokinase. Biochemistry 26, 4143-4148.
124. Lawson, C. & Sigler, P.B. (1988). The structure of trp pseudorepressor at 165 A shows why indol propionate acts as a trp ‘inducer’. Nature 333, 869-871.
125. Lawson, C. L., Zhang, R.-G., Schevitz, R. W., Otwinowski, Z., Joachimiak, A. & Sigler, P.B. (1988). Flexibility of the DNA-binding domains of trp repressor. Proteins 3, 18-31.
126. Lear, J. D., Wasserman, Z.R. & Degrade, W.F. (1988). Synthetic amphiphilic peptide models for protein ion channels. Science 240, 1177-1181.
127. Leonard, R. J., Labarca, C. G., Charnet, P., Davidson, N. & Lester, H.A. (1988). Evidence that the M2 spanning region lines the ion channel pore of the nicotinic receptor. Science 242, 1578-1581.
128. Liddington, R., Derewenda, Z., Dodson, G. & Harris, D. (1988). Structure of liganded T-state of haemoglobin identifies the origin of cooperative oxygen binding. Nature 331, 725-728.
129. Linzen, B., Soeter, N. M., Riggs, A. F., Schneider, H.-J., Schartau, W., Moore, M. D., Yokota, E., Behrens, P. Q., Nakashima, H., Takagi, T., Nemoto, T., Vereijken, J. M., Bak, H. J., Beintema, J. J., Volbeda, A., Gaykema, W.P.J. & Hol. W.G.J. (1985). The structure of arthropod haemocyanins. Science, N.Y. 229, 519-524.
130. Louie, G., Tran, T., Englander, J.J. & Englander, S.W. (1988). Allosteric energy at the hemoglobin B-chain C-terminus studied by hydrogen exchange. J. molec. Biol. 201,755-764.
131. Mcgeoch, D., Mcgeoch, J. & Morse, D. (1973). Synthesis of tryptophan operon RNA in a cell-free system. Nature New Biol. 245, 137-140.
132. Mclaughlin, P. J., Stuart, D. I., Klein, H. W., Oinomakos, J.G. & Johnson, L. N.(1984). Substrate cofactor interactions for glycogen phosphorylase b: A binding study in the crystal with heptenitol and heptulose-2-phosphate. Biochemistry 23, 5862-5873.
133. Madsen, N.B. (1986). Glycogen phosphorylase. In The Enzymes, 3rd ed., vol. 17 (ed. P.D. Boyer and E.G. Krebs), pp. 366-394. New York: Academic Press.
134. Manwell, C. (1960). Oxygen equilibrium of the brachiopod Lingula hemerythrin. Science 132, 550-551.
135. Marmorstein, R.Q. & Sigler, P.B. (1988). Structure and mechanism of the trp repressor/operator system. In Nucleic Acids and Molecular Biology (ed. F. Eckstein). Heidelberg. Springer-Verlag.
136. Marmorstein, R. Q., Joachimiak, A., Sprinzl, M. & Sigler, P.B. (1987). The structural basis for the interaction between L-tryptophan and the Escherichia coli trpaporepressor. J. biol. Chem. 262, 4922-4927.
137. Matsukawa, S., Itatani, Y., Mawatari, K., Shimokawa, Y. & Yoneyama, Y. (1978). Quantitative evaluation for the role fi-itft His and /ff-143 His residues in the Bohr effect of human haemoglobin in the presence of o-i M chloride Ion. J. biol. Chem. 259, 11479-11486.
138. Messana, C., Cerdonio, M., Shenkin, P., Noble, R. W., Fermi, G., Perutz, R.N. & Perutz, M.F. (1978). Influence of quaternary structure of the globin on thermal spin equilibria in different methaemoglobin derivatives. Biochemistry 17, 3652-3662.
139. Middleton, S.A. & Kantrowitz, E.R. (1988). Function of arginine-234 and aspartic acid-271 in domain closure, cooperativity, and catalysis in Escherichia coli aspartate transcarbamylase. Biochemistry 27, 8653-8660.
140. Miller, K.I. (1985). Oxygen equilibria of Octopus dofleini hemocyanin. Biochemistry 24, 4582-4586.
141. Momenteau, M., Scheidt, W. R., Elgenbrot, C.W. & Reed, C.A. (1988). A deoxymyoglobin model with a sterically unhindered axial imidazole. J. Am. Chem. Soc., 1207-1215.
142. Monod, J., Changeux, J.P. & Jacob, F. (1963). Allosteric proteins and molecular control systems. J. molec. Biol. 6, 306-329.
143. Monod, J. & Cohen-Bazire, G. (1953). L'efTet d'inhibition specifique dans la biosynthese de la tryptophane-desmase chez Aerobacter aerogenus. C.R. Hebd. Seanc. Acad. Sci., Paris 236, 530-532.
144. Monod, J. & Jacob, F. (1961). Genetic regulation mechanisms in the synthesis of proteins. J. molec. Biol. 3, 318-356.
145. Monod, J., Wyman, J. & Changeux, J.P. (1965). On the nature of allosteric transitions: A plausible model. J. molec. Biol. 12, 88-118.
146. Namba, K., Pattanayek, R. & Stubbs, G. (1989). Visualization of protein-nucleic acid interactions in a virus: Refined structure of intact tobacco mosaic virus at 2-9 A resolution by X-ray diffraction. J. molec. Biol. 208, 307-325.
147. Newell, J. O., Markby, D.W. & Schachman, H.K. (1989). Cooperative binding of the bisubstrate analog AT-(phosphonacetyl)-L-aspartate to aspartate transcarbamylase and the heterotropic effects of ATP and CTP.J. biol. Chem. 264, 2476-2481.
148. Oiki, S., Danho, W., Madison, V. & Montal, M. (1988). M2 S., a candidate for the structure lining the ionic channel of the nicotinic cholinergic receptor. Proc. natn. Acad. Sci. U.S.A. 85, 8703-8707.
149. Olson, J. S., Mathews, A. J., Rohlfs, R. J., Springer, B. A., Edelberg, K. D., Sliger, S. G., Tame, J., Renaud, J.-P. & Nagai, K. (1988). The role of the distalhistidine in myoglobin and haemoglobin. Nature 336, 265-266.
150. Philo, S. & Dreyer, U. (1985). Quarternary structure has little influence on spin states in mixed-spin human methemoglobins. Biochemistry 24, 2985-2991.
151. Ptashne, M. (1986). A Genetic Switch. Cambridge, Mass.: Cell Press; Oxford: Blackwell Scientific Publications.
152. Robinson, I.K. & Harrison, S.C. (1982). Structure of the expanded state of tobacco bushy stunt virus. Nature 297, 563-568.
153. Schachman, H.K. (1988). Can a simple model account for the allosteric transition of aspartate transcarbamylase ? J. biol. Chem. 263, 18583-18586.
154. Stadtman, E.R. & Ginsburg, A. (1974). The glutamine synthetase of Escherichia colt: Structure and control. In The Enzymes, vol. io, pp. 755-808. New York: Academic Press.
155. Stencamp, R. E., Sieker, L. C., Jensen, L. H., Mccallum, J.D. & Sanders-Loehr, J. (1985). Active site structures of deoxyhemerythrin and oxyhemerythrin. Proc. natn. Acad. Sci. U.S.A. 82, 713-716.
156. Unwin, P.N.T. & Zampighi, G. (1980). Structure of the junction between communicating cells. Nature 283, 545.
157. Van Holde, K.E. & Miller, K.I. (1982). Haemocyanins. Q. Rev. Biophys. 15, 1-129.
158. Weber, K. (1968). A new structural model of Escherichia coli aspartate transcarbamylase and the amino acid sequence of the regulatory chain. Nature 218, 1116-1119.
159. Wyman, J. (1984). Linkage graphs: A study in the thermodynamics of macromolecules. Q. Rev. Biophys. 17, 453-488.
160. Yamashita, M. M., Almassy, R. J., Janson, C. A., Cascio, D. & Eisenberg, D. (1989). Refined atomic model of glutamine synthetase at 3-5 A resolution. J. biol. Chem. (In the Press.)
161. Yates, R.A. & Pardee, A.B. (1956). Control of pyrimidine biosynthesis in Escherichia coli by a feedback mechanism. J. biol. Chem. 221, 757-770.
162. Zhang, K., Stern, E. A., Ellis, F., Sanders-Loehr, J. & Shiemke, A.K. (1988). The active site of hemerythrin as determined by X-ray Absorption Fine Structure. Biochemistry 27, 7470-7479.
163. Zhang, R.-G., Joachimiak, A., Lawson, C. L., Schevitz, R. W., Otwinowski, Z. & Sigler, P.B. (1987). The crystal structure of trp aporepressor at r-8 A shows how binding tryptophan enhances DNA affinity. Nature 327, 591-597.
164. Zubay, G., Morse, D. E., Schrenk, W.J. & Miller, J.H.M. (1972). Detection and isolation of the repressor protein for the tryptophan operator of Escherichia coli. Proc. natn. Acad. Sci. U.S.A. 69, 1100-1103.