Multiple Conformations of E. coli Hsp90 in Solution: Insights into the Conformational Dynamics of Hsp90

Structure

Volumn 16, Issue 5, 2008, Pages 755-765

  Krukenberg, Kristin A ^a   Förster, Friedrich ^b   Rice, Luke M ^a   Sali, Andrej ^b   Agard, David A ^a  

^a HOWARD HUGHES MEDICAL INSTITUTE   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

PROTEINS

Indexed keywords

HEAT SHOCK PROTEIN 90; NUCLEOTIDE;

ARTICLE; CONFORMATION; CRYSTAL STRUCTURE; EQUILIBRIUM CONSTANT; ESCHERICHIA COLI; MOLECULAR DYNAMICS; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; SOLUTION AND SOLUBILITY; X RAY CRYSTALLOGRAPHY;

ADENYLYL IMIDODIPHOSPHATE; DIMERIZATION; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HSP90 HEAT-SHOCK PROTEINS; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SCATTERING, SMALL ANGLE; SOLUTIONS; X-RAY DIFFRACTION;

BACTERIA (MICROORGANISMS); EUKARYOTA;

EID: 42949147146     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2008.01.021     Document Type: Article

References (36)

1. Ali M.M., Roe S.M., Vaughan C.K., Meyer P., Panaretou B., Piper P.W., Prodromou C., and Pearl L.H. Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex. Nature 440 (2006) 1013-1017
2. Caplan A.J., Mandal A.K., and Theodoraki M.A. Molecular chaperones and protein kinase quality control. Trends Cell Biol. 17 (2007) 87-92
3. Chiosis G., Lucas B., Huezo H., Solit D., Basso A., and Rosen N. Development of purine-scaffold small molecule inhibitors of Hsp90. Curr. Cancer Drug Targets 3 (2003) 371-376
4. Debye P. Zerstreuung von roentgenstrahlen. Annalen der Physik 46 (1915) 809-823
5. Dollins D.E., Warren J.J., Immormino R.M., and Gewirth D.T. Structures of GRP94-nucleotide complexes reveal mechanistic differences between the Hsp90 chaperones. Mol. Cell 28 (2007) 41-56
6. Fang L., Ricketson D., Getubig L., and Darimont B. Unliganded and hormone-bound glucocorticoid receptors interact with distinct hydrophobic sites in the Hsp90 C-terminal domain. Proc. Natl. Acad. Sci. USA 103 (2006) 18487-18492
7. Feltham J.L., and Gierasch L.M. GroEL-substrate interactions: molding the fold, or folding the mold. Cell 100 (2000) 193-196
8. Fraser R.D.B., MacRae T.P., and Suzuki E. An improved method for calculating the contribution of solvent to the X-ray diffraction pattern of biological molecules. J. Appl. Crystallogr. 11 (1978) 693-694
9. Freeman B.C., and Yamamoto K.R. Disassembly of transcriptional regulatory complexes by molecular chaperones. Science 296 (2002) 2232-2235
10. Frey S., Leskovar A., Reinstein J., and Buchner J. The ATPase cycle of the endoplasmic chaperone Grp94. J. Biol. Chem. 282 (2007) 35612-35620
11. Grantcharova V., Alm E.J., Baker D., and Horwich A.L. Mechanisms of protein folding. Curr. Opin. Struct. Biol. 11 (2001) 70-82
12. Huai Q., Wang H., Liu Y., Kim H.Y., Toft D., and Ke H. Structures of the N-terminal and middle domains of E. coli Hsp90 and conformation changes upon ADP binding. Structure 13 (2005) 579-590
13. Konarev P.V., Volkov V.V., Sokolova A.V., Koch M.H.J., and Svergun D.I. PRIMUS: a Windows PC-based system for small-angle scattering data analysis. J. Appl. Crystallogr. 36 (2003) 1277-1282
14. MacKerell Jr. A.D., Bashford D., Bellot M., Dunbrack Jr. R.L., Evanseck J.D., Field M.J., Fischer S., Gao J., Guo H., Ha S., et al. All-atom empirical potential for molecular modeling and dynamic studies of proteins. J. Phys. Chem. B 102 (1998) 3586-3616
15. Madauss K.P., Deng S.J., Austin R.J., Lambert M.H., McLay I., Pritchard J., Short S.A., Stewart E.L., Uings I.J., and Williams S.P. Progesterone receptor ligand binding pocket flexibility: crystal structures of the norethindrone and mometasone furoate complexes. J. Med. Chem. 47 (2004) 3381-3387
16. Mayer M.P., and Bukau B. Hsp70 chaperones: cellular functions and molecular mechanism. Cell. Mol. Life Sci. 62 (2005) 670-684
17. Neckers L. Heat shock protein 90: the cancer chaperone. J. Biosci. 32 (2007) 517-530
18. Neckers L., and Ivy S.P. Heat shock protein 90. Curr. Opin. Oncol. 15 (2003) 419-424
19. Pearl L.H., and Prodromou C. Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu. Rev. Biochem. 75 (2006) 271-294
20. Picard D. Heat-shock protein 90, a chaperone for folding and regulation. Cell. Mol. Life Sci. 59 (2002) 1640-1648
21. Picard D. Chaperoning steroid hormone action. Trends Endocrinol. Metab. 17 (2006) 229-235
22. Pratt W.B., and Toft D.O. Regulation of signaling protein function and trafficking by the Hsp90/Hsp70-based chaperone machinery. Exp. Biol. Med. (Maywood) 228 (2003) 111-133
23. Richter K., and Buchner J. Hsp90: chaperoning signal transduction. J. Cell. Physiol. 188 (2001) 281-290
24. Sali A., and Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234 (1993) 779-815
25. Shen M.Y., and Sali A. Statistical potential for assessment and prediction of protein structures. Protein Sci. 15 (2006) 2507-2524
26. Shiau A.K., Harris S.F., Southworth D.R., and Agard D.A. Structural analysis of E. coli Hsp90 reveals dramatic nucleotide-dependent conformational rearrangements. Cell 127 (2006) 329-340
27. Svergun D.I. Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J. Appl. Crystallogr. 25 (1992) 495-503
28. Svergun D.I. Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys. J. 76 (1999) 2879-2886
29. Svergun D.I., Petoukhov M.V., and Koch M.H.J. Determination of domain structure of proteins from X-ray solution scattering. Biophys. J. 80 (2001) 2946-2953
30. White H.D., and Taylor E.W. Energetics and mechanism of actomyosin adenosine triphosphatase. Biochemistry 15 (1976) 5818-5826
31. Whitesell L., and Lindquist S.L. Hsp90 and the chaperoning of cancer. Nat. Rev. Cancer 5 (2005) 761-772
32. Workman P. Altered states: selectively drugging the Hsp90 cancer chaperone. Trends Mol. Med. 10 (2004) 47-51
33. Young J.C., Moarefi I., and Hartl F.U. Hsp90: a specialized but essential protein-folding tool. J. Cell Biol. 154 (2001) 267-273
34. Young J.C., Agashe V.R., Siegers K., and Hartl F.U. Pathways of chaperone-mediated protein folding in the cytosol. Nat. Rev. Mol. Cell Biol. 5 (2004) 781-791
35. Zhang W., Hirshberg M., McLaughlin S.H., Lazar G.A., Grossmann J.G., Nielsen P.R., Sobott F., Robinson C.V., Jackson S.E., and Laue E.D. Biochemical and structural studies of the interaction of Cdc37 with Hsp90. J. Mol. Biol. 340 (2004) 891-907
36. Zhao R., Davey M., Hsu Y.C., Kaplanek P., Tong A., Parsons A.B., Krogan N., Cagney G., Mai D., Greenblatt J., et al. Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the Hsp90 chaperone. Cell 120 (2005) 715-727