The sugar kinase/heat shock protein 70/actin superfamily: Implications of conserved structure for mechanism

Annual Review of Biophysics and Biomolecular Structure

Volumn 25, Issue , 1996, Pages 137-162

  Hurley, James H ^a  

^a NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

Author keywords

conformational change; enzyme mechanism; enzyme regulation; protein structure; X ray crystallography

Indexed keywords

ACTIN; ADENOSINE TRIPHOSPHATE; CALCIUM ION; CHAPERONE; HEAT SHOCK PROTEIN 70; MAGNESIUM ION; PROTEIN KINASE;

ACTIN FILAMENT; BINDING SITE; CATALYSIS; CONFORMATIONAL TRANSITION; HYDROGEN BOND; HYDROLYSIS; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN FOLDING; REVIEW;

EID: 0029948487     PISSN: 10568700     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.bb.25.060196.001033     Document Type: Review

References (75)

1. Anderson CM, Steitz TA. 1975. Structure of yeast hexokinase IV. Low-resolution structure of enzyme-substrate complexes revealing negative co-operativity and allosteric interactions. J. Mol. Biol. 92:279-87
2. Anderson CM, Stenkamp RE, McDonald RC, Steitz TA. 1978. A refined model of the sugar binding site of yeast hexokinase Br. J. Mol. Biol. 123: 207-19
3. Bennett WS, Steitz TA. 1980. Structure of a complex between yeast hexokinase A and glucose. I. Structure determination and refinement at 3.5 Å resolution. J. Mol. Biol. 140:183-209
4. Bennett WS, Steitz TA. 1980. Structure of a complex between yeast hexokinase A and glucose. II. Detailed comparisons of conformation and active site configuration with the native hexokinase B monomer and dimer. J. Mol. Biol. 140:211-30
5. 18O]triphosphate and the mechanistic consequences for the reactions catalyzed by glycerol kinase, hexokinase, pyruvate kinase, and acetate kinase. Biochemistry 18:3927-33
6. 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. USA 89: 7290-94
7. Bork P, Sander C, Valencia A. 1993. Convergent evolution of similar enzymatic function on different protein folds: the hexokinase, ribokinase, and galactokinase families of sugar kinases. Protein Sci. 2:31-40
8. Bremer A, Aebi U. 1992. The structure of the F-actin filament and the actin molecule. Curr. Opin. Cell Biol. 4: 20-26
9. Buchberger A, Valencia A, McMacken R, Sander C, Bernd B. 1994. The chaperone function of DnaK requires the coupling of ATPase activity with substrate binding through residue E171. EMBO J. 13:1687-95
10. Buchberger A, Valencia A, McMacken R, Sander C, Bernd B. 1994. A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE. Nat. Struct. Biol. 1:95-101
11. Carlier M-F. Actin: protein structure and filament dynamics. 1991. J. Biol. Chem. 266:1-4
12. Craig EA, Weissman JS, Horwich AL. 1994. Heat shock proteins and molecular chaperones: mediators of protein conformation and turnover in the cell. Cell 78:365-72
13. Cyr DM, Lu X, Douglas MG. 1992. Regulation of Hsp70 function by a eukaryotic DnaJ homolog. J. Biol. Chem. 267:20927-31
14. Dannenburg KD, Cleland WW. 1975. Use of chromium-adenosine triphosphate and lyxose to elucidate the kinetic mechanism and coordination state of the nucleotide substrate for yeast hexokinase. Biochemistry 14: 28-39
15. DelaFuente G, Lagunas R, Sols A. 1970. Induced fit in yeast hexokinase. Eur. J. Biochem. 16:226-33
16. Derechin M, Rustum YM, Barnard EA. 1972. Dissociation of yeast hexokinase under the influence of substrates. Biochemistry 11:1793-97
17. deRiel JK, Paulus H. 1978. Subunit dissociation in the allosteric regulation of glycerol kinase from Escherichia coll. 1. Kinetic evidence. Biochemistry 17:5134-40
18. deRiel JK, Paulus H. 1978. Subunit dissociation in the allosteric regulation of glycerol kinase from Escherichia coli. 2. Physical evidence. Biochemistry 17:5141-45
19. Drewes G, Faulstich H. 1991. A reversible cpnformational transition in muscle actin is caused by nucleotide exchange and uncovers cysteine in position 10. J. Biol. Chem. 266:5508-13
20. Feldman I, Kramp DC. 1978. Fluorescence-quenching study of glucose binding by yeast hexokinase isoenzymes. Biochemistry 17:1541-47
21. Flaherty KM, DeLuca-Flaherty C, McKay DB. 1990. Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein. Nature 346:623-28
22. Flaherty KM, McKay DB, Kabsch W, Holmes KC. 1991. Similarity of the three-dimensional structures of actin and the ATPase fragment of a 70-kDa heat shock cognate protein. Proc. Natl. Acad. Sci. USA 88:5041-45
23. Flaherty KM, Wilbanks SM, DeLuca-Flaherty C, McKay DB. 1994. Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. II. Structure of the active site with ADP or ATP bound to wild type and mutant ATPase fragment. J. Biol. Chem. 269:12899-907
24. Frohlick K-U, Entian KD, Mecke D. 1985. The primary structure of the yeast hexokinase PII gene (HXK2) which is responsible for glucose repression. Gene 36:105-11
25. Gao B, Greene L, Eisenberg E. 1994. Characterization of nucleotide-free uncoating ATPase and its binding to ATP, ADP, and ATP analogues. Biochemistry 33:2048-54
26. Georgopoulos C. 1992. The emergence of the chaperone machines. Trends Biochem. Sci. 17:295-99
27. Gething M-J, Sambrook J. 1992. Protein folding in the cell. Nature 355: 33-45
28. Goldschmidt-Clermont PJ, Machesky LM, Doberstein SK, Pollard TD. 1991. Mechanism of the interaction of human platelet profilin with actin. J. Cell. Biol. 113:1081-89
29. Ha J-H, McKay DB. 1994. ATPase kinetics of recombinant bovine 70 kDa heat shock cognate protein and its amino-terminal ATPase domain. Biochemistry 33:14625-35
30. Hendrick JP, Hartl FU. 1993. Molecular chaperone functions of heat-shock proteins. Anna. Rev. Biochem. 62: 349-84
31. Hoggett JG, Kellett GL. 1976. Yeast hexokinase: substrate-induced association-dissociation reactions in the binding of glucose to hexokinase P-II. Eur. J. Biochem. 66:65-77
32. Holmes KC, Popp D, Gebhard W, Kabsch W. 1990. Atomic model of the actin filament. Nature 347:44-49
33. Huang S-P, Tsai M-Y, Tzou Y-M, Wu W-G, Wang C. 1993. Aspartyl residue 10 is essential for ATPase activity of rat hsc70. J. Biol. Chem. 268:2063-68
34. Glc with glycerol kinase. Science 259:673-77
35. Janmey PA, Hvidt S, Oster GF, Lamb J, Stossel TP, et al. 1990. Effect of ATP on actin filament stiffness. Nature 347:95-99
36. 18O isotope effects for hexokinase-catalyzed phpsphoryl transfer from ATP. Biochemistry 30: 3634-39
37. Kabsch W, Holmes KC. 1995. The actin fold. FASEB J. 9:167-74
38. Kabsch W, Mannherz HG, Suck D, Pai EF, Holmes KC. 1990. Atomic structure of the actin: DNase I complex. Nature 347:37-44
39. Kabsch W, Vandekerckhove J. 1992. Structure and function of actin. Annu. Rev. Biophys. Biomol. Struct. 21: 49-76
40. Kaji A, Colowick SP. 1965. Adenosine triphosphatase activity of yeast hexokinase and its relation to the mechanism of the hexokinase reaction. J. Biol. Chem. 240:4454-62
41. Korn ED, Carlier M-F, Pantaloni D. 1987. Actin polymerization and ATP hydrolysis. Science 238:638-44
42. Knight WB, Cleland WW. 1989. Thiol and amino analogues as alternate substrates for glycerokinase from Candida mycoderma. Biochemistry 28: 5728-34
43. Lesk AM, Chothia C. 1984. Mechanisms of domain closure in proteins. J. Mol. Biol. 174:175-91
44. Liberbek K, Skowyra D, Zylicz M, Johnson C, Georgopolous C. 1991. The Escherichia coli DnaK chaperone, the 70-kDa heat shock protein eukaryotic equivalent, changes conformation upon ATP hydrolysis, thus triggering its dissociation from a bound target protein. J. Biol. Chem. 266:14491-96
45. Glc. Biochemistry 33:10120-26
46. Lorenz M, Popp D, Holmes KC. 1993. Refinement of the F-actin model against x-ray fiber diffraction data by the use of a directed mutation algorithm. J. Mol. Biol. 234:826-36
47. McCarty JS, Buchberger A, Reinstein J, Bukau B. 1995. The role of ATP in the functional cycle of the DnaK chaperone system. J. Mol. Biol. 249: 126-37
48. McDonald RC, Steitz TA, Engelman DM. 1979. Yeast hexokinase in solution exhibits a large conformational change upon binding glucose or glucose 6-phosphate. Biochemistry 18: 338-42
49. McKay DB. 1993. Structure and mechanism of 70-kDa heat-shock-related proteins. Adv. Protein Chem. 44: 67-98
50. McLaughlin PJ, Gooch JT, Mannherz HG, Weeds HG. 1993. Structure of gelsolin segment 1-actin complex and the mechanism of filament severing, Nature 364:685-92
51. Miki M, Kouyama T. 1994. Domain motion in actin observed by fluorescence resonance energy transfer. Biochemistry 33:1017-77
52. Glc of the phosphotransferase system in Escherichia coli and Salmonella typhimurium. J. Bacteriol. 162: 810-16
53. O'Brien MC, McKay DB. 1993. Threonine 204 of the chaperone protein Hsc70 influences the structure of the active site, but is not essential for ATP hydrolysis. J. Biol. Chem. 268: 24323-29
54. + but not ATP hydrolysis. Nature 365:664-66
55. Palleros DR, Welch WJ, Fink AL. 1991. Interaction of hsp70 with unfolded proteins: effects of temperature and nucleotides on the kinetics of binding. Proc. Natl. Acad. Sci. USA 88:5719-23
56. Peters BA, Neet KE. 1978. Yeast hexokinase PII. Conformational changes induced by substrates and substrate analogues. J. Biol. Chem. 253:6826-31
57. Pettigrew DW, Yu GY, Liu Y. 1990. Nucleotide regulation of Escherichia coli glycerol kinase: initial-velocity and substrate binding studies. Biochemistry 29:8620-27
58. Pollard TD. 1990. Actin. Curr. Opin. Cell Biol. 2:33-40
59. Rose IA, O'Connell EL, Litwin S, Bar Tana J. 1974. Determination of the rate of hexokinase-glucose dissociation by the isotope-trapping method. J. Biol. Chem. 249:5163-68
60. Rudolph FB, Fromm HJ. 1971. Computer simulation studies with yeast hexokinase and additional evidence for the random bi bi mechanism. J. Biol. Chem. 246:6611-19
61. Sadis S, Hightower LE. 1992. Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange. Biochemistry 31:9407-12
62. Schmid D, Baici A, Gehring H, Christen P. 1994. Kinetics of molecular chaperone action. Science 263:971-73
63. Schutt CE, Myslik JC, Rozycki MD, Goonesekere NCW, Lindberg U. 1993. The structure of crystalline profilin-β-actin. Nature 365:810-16
64. Sheterline P, Sparrow JC. 1994. Actin. Protein Profile 1:1-100
65. Shill JP, Neet KE. 1975. Allosteric properties and the slow transition of yeast hexokinase. J. Biol. Chem. 250: 2259-68
66. Steitz TA, Fletterick RJ, Anderson WF, Anderson CM. 1976. High resolution x-ray structure of yeast hexokinase, an allosteric protein exhibiting a non-symmetric arrangement of subunits. J. Mol. Biol. 104:197-222
67. Szabo A, Langer T, Schroder H, Flanagan J, Bukau B, et al. 1994. The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system-DnaK, DnaJ, and GrpE. Proc. Natl. Acad. Sci. USA 91:10345-49
68. Thorner JW, Paulus H. 1971. Composition and subunit structure of glycerol kinase from Escherichia coli. J. Biol. Chem. 246:3885-94
69. Thorner JW, Paulus H. 1973. Catalytic and allosteric properties of glycerol kinase from Escherichia coli. J. Biol. Chem. 248:3922-32
70. Tirion MM, ben-Avraham D. 1993. Normal mode analysis of G-actin. J. Mol. Biol. 230:186-95
71. Vanderkerckove J. 1990. Actin-binding proteins. Curr. Opin. Cell Biol. 2: 41-50
72. Viola RE, Cleland WW. 1978. Use of pH studies to elucidate the chemical mechanism of yeast hexokinase. Biochemistry 17:4111-17
73. Viola RE, Raushel FM, Rendina AR, Cleland WW. 1982. Substrate synergism and the kinetic mechanism of yeast hexokinase. Biochemistry 21: 1295-1302
74. Wilbanks SM, DeLuca-Flaherty C, McKay DB. 1994. Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. I. Kinetic analyses of active site mutants. J. Biol. Chem. 269:12893-98
75. Wilbanks SM, McKay DB. 1995. How potassium affects the activity of the molecular chaperone Hsc70. II. Potassium binds specifically in the ATPase active site. J. Biol. Chem. 270: 2251-57