Crystal structures of a group II chaperonin reveal the open and closed states associated with the protein folding cycle

Journal of Biological Chemistry

Volumn 285, Issue 36, 2010, Pages 27958-27966

  Pereira, Jose H ^a   Ralston, Corie Y ^a   Douglas, Nicholai R ^b   Meyer, Daniel ^b,e   Knee, Kelly M ^c   Goulet, Daniel R ^c   King, Jonathan A ^c   Frydman, Judith ^b   Adams, Paul D ^a,d  

^a LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

^b STANFORD UNIVERSITY   (United States)

^c MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^d University of California at Berkeley   (United States)

^e MAX PLANCK INSTITUTE OF NEUROBIOLOGY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN FOLDING;

APICAL DOMAIN; ARCHAEAL; CHAPERONIN; CLOSE-IN; EQUATORIAL DOMAIN; GROUP II CHAPERONINS; HYDROPHILIC SURFACES; LARGE ROTATION; METHANOCOCCUS MARIPALUDIS; MULTISUBUNIT; OPEN CONFORMATION; PROTEIN COMPLEXES; RIGID BODY;

CRYSTAL STRUCTURE;

CHAPERONIN; ADENOSINE TRIPHOSPHATE;

ARTICLE; BINDING SITE; CONTROLLED STUDY; CRYSTAL STRUCTURE; HYDROPHILICITY; METHANOCOCCUS MARIPALUDIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; CHEMICAL STRUCTURE; CHEMISTRY; HYDROLYSIS; METABOLISM; METHANOCOCCUS; PROTEIN TERTIARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

ARCHAEA; METHANOCOCCUS MARIPALUDIS;

ADENOSINE TRIPHOSPHATE; CRYSTALLOGRAPHY, X-RAY; GROUP II CHAPERONINS; HYDROLYSIS; METHANOCOCCUS; MODELS, MOLECULAR; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY;

EID: 77956256437     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.125344     Document Type: Article

References (58)

1. Frydman, J. (2001) Annu. Rev. Biochem. 70, 603-647
2. Taubes, G. (1996) Science 271, 1493-1495
3. Dobson, C. M. (2004) Semin. Cell Dev. Biol. 15, 3-16
4. Reissmann, S., Parnot, C., Booth, C. R., Chiu, W., and Frydman, J. (2007) Nat. Struct. Mol. Biol. 14, 432-440
5. Booth, C. R., Meyer, A. S., Cong, Y., Topf, M., Sali, A., Ludtke, S. J., Chiu, W., and Frydman, J. (2008) Nat. Struct. Mol. Biol. 15, 746-753
6. Horwich, A. L., Farr, G. W., and Fenton, W. A. (2006) Chem. Rev. 106, 1917-1930
7. Frydman, J., Nimmesgern, E., Erdjument-Bromage, H., Wall, J. S., Tempst, P., and Hartl, F. U. (1992) EMBO J. 11, 4767-4778
8. Shomura, Y., Yoshida, T., Iizuka, R., Maruyama, T., Yohda, M., and Miki, K. (2004) J. Mol. Biol. 335, 1265-1278
9. Chen, S., Roseman, A. M., Hunter, A. S., Wood, S. P., Burston, S. G., Ranson, N. A., Clarke, A. R., and Saibil, H. R. (1994) Nature 371, 261-264
10. Roseman, A. M., Chen, S., White, H., Braig, K., and Saibil, H. R. (1996) Cell 87, 241-251
11. Clare, D. K., Bakkes, P. J., van Heerikhuizen, H., van der Vies, S. M., and Saibil, H. R. (2009) Nature 457, 107-110
12. Braig, K., Otwinowski, Z., Hegde, R., Boisvert, D. C., Joachimiak, A., Horwich, A. L., and Sigler, P. B. (1994) Nature 371, 578-586
13. Chaudhry, C., Horwich, A. L., Brunger, A. T., and Adams, P. D. (2004) J. Mol. Biol. 342, 229-245
14. Hunt, J. F., Weaver, A. J., Landry, S. J., Gierasch, L., and Deisenhofer, J. (1996) Nature 379, 37-45
15. Mande, S. C., Mehra, V., Bloom, B. R., and Hol, W. G. (1996) Science 271, 203-207
16. Braig, K., Adams, P. D., and Brünger, A. T. (1995) Nature Struct. Biol. 2, 1083-1094
17. Xu, Z., Horwich, A. L., and Sigler, P. B. (1997) Nature 388, 741-750
18. Lin, Z., Schwartz, F. P., and Eisenstein, E. (1995) J. Biol. Chem. 270, 1011-1014
19. Chen, L., and Sigler, P. B. (1999) Cell 99, 757-768
20. Weissman, J. S., Hohl, C. M., Kovalenko, O., Kashi, Y., Chen, S., Braig, K., Saibil, H. R., Fenton, W. A., and Horwich, A. L. (1995) Cell 83, 577-587
21. Mayhew, M., da Silva, A. C., Martin, J., Erdjument-Bromage, H., Tempst, P., and Hartl, F. U. (1996) Nature 379, 420-426
22. Roseman, A. M., Ranson, N. A., Gowen, B., Fuller, S. D., and Saibil, H. R. (2001) J. Struct. Biol. 135, 115-125
23. Weissman, J. S., Kashi, Y., Fenton, W. A., and Horwich, A. L. (1994) Cell 78, 693-702
24. Ranson, N. A., Burston, S. G., and Clarke, A. R. (1997) J. Mol. Biol. 266, 656-664
25. Horovitz, A., Fridmann, Y., Kafri, G., and Yifrach, O. (2001) J. Struct. Biol. 135, 104-114
26. Saibil, H. R., Horwich, A. L., and Fenton, W. A. (2001) Adv. Protein Chem. 59, 45-72
27. Swain, J. F., and Gierasch, L. M. (2006) Curr. Opin. Struct. Biol. 16, 102-108
28. Kafri, G., and Horovitz, A. (2003) J. Mol. Biol. 326, 981-987
29. Yifrach, O., and Horovitz, A. (1998) Biochemistry 37, 7083-7088
30. Yifrach, O., and Horovitz, A. (1995) Biochemistry 34, 5303-5308
31. Kafri, G., Willison, K. R., and Horovitz, A. (2001) Protein Sci. 10, 445-449
32. Ditzel, L., Löwe, J., Stock, D., Stetter, K. O., Huber, H., Huber, R., and Steinbacher, S. (1998) Cell 93, 125-138
33. Jancarik, J., and Kim, S. H. (1991) J. Appl. Cryst. 24, 409-411
34. Otwinowski, Z., and Minor, W. (1997) in Methods Enzymology: Macromolecular Crystallography (Carter, C. W., and Sweet, R. M., eds) Vol. 276, pp. 307-326, Academic Press, New York
35. McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., and Read, R. J. (2007) J. Appl. Crystallogr. 40, 658-674
36. DeLaBarre, B., and Brunger, A. T. (2006) Acta Crystallogr. D Biol. Crystallogr. 62, 923-932
37. Ling, H., Boodhoo, A., Hazes, B., Cummings, M. D., Armstrong, G. D., Brunton, J. L., and Read, R. J. (1998) Biochemistry 37, 1777-1788
38. Adams, P. D., Grosse-Kunstleve, R. W., Hung, L. W., Ioerger, T. R., McCoy, A. J., Moriarty, N. W., Read, R. J., Sacchettini, J. C., Sauter, N. K., and Terwilliger, T. C. (2002) Acta Crystallogr. D Biol. Crystallogr. 58, 1948-1954
39. Afonine, P. V., Grosse-Kunstleve, R. W., Urzhumtsev, A., and Adams, P. D. (2009) J. Appl. Crystallogr. 42, 607-615
40. Emsley, P., and Cowtan, K. (2004) Acta Crystallogr. D. Biol Crystallogr. 60, 2126-2132
41. Davis, I. W., Leaver-Fay, A., Chen, V. B., Block, J. N., Kapral, G. J., Wang, X., Murray, L. W., Arendall, W. B., 3rd, Soeyink, J., Richardson, J. C., and Richardson, D. C. (2007) Nucleic Acids Res. 35, 375-383
42. Llorca, O., Smyth, M. G., Carrascosa, J. L., Willison, K. R., Radermacher, M., Steinbacher, S., and Valpuesta, J. M. (1999) Nat. Struct. Biol. 6, 639-642
43. Nitsch, M., Walz, J., Typke, D., Klumpp, M., Essen, L. O., and Baumeister, W. (1998) Nat. Struct. Biol. 5, 855-857
44. Gutsche, I., Holzinger, J., Rössle, M., Heumann, H., Baumeister, W., and May, R. P. (2000) Curr. Biol. 10, 405-408
45. Gutsche, I., Holzinger, J., Rauh, N., Baumeister, W., and May, R. P. (2001) J. Struct. Biol. 135, 139-146
46. Iizuka, R., Yoshida, T., Shomura, Y., Miki, K., Maruyama, T., Odaka, M., and Yohda, M. (2003) J. Biol. Chem. 278, 44959-44965
47. Clare, D. K., Stagg, S., Quispe, J., Farr, G. W., Horwich, A. L., and Saibil, H. R. (2008) Structure 16, 528-534
48. Zhang, J., Baker, M. L., Schröder, G. F., Douglas, N. R., Reissmann, S., Jakana, J., Dougherty, M., Fu, C. J., Levitt, M., Ludtke, S. J., Frydman, J., and Chiu, W. (2010) Nature 463, 379-383
49. Saraste, M., Sibbald, P. R., and Wittinghofer, A. (1990) Trends Biochem. Sci. 15, 430-434
50. Rommelaere, H., De Neve, M., Melki, R., Vandekerckhove, J., and Ampe, C. (1999) Biochemistry 38, 3246-3257
51. Feldman, D. E., Spiess, C., Howard, D. E., and Frydman, J. (2003) Mol. Cell 12, 1213-1224
52. Kubota, S., Kubota, H., and Nagata, K. (2006) Proc. Natl. Acad. Sci. U.S.A. 103, 8360-8365
53. Spiess, C., Meyer, A. S., Reissmann, S., and Frydman, J. (2004) Trends Cell Biol. 14, 598-604
54. Sewell, B. T., Best, R. B., Chen, S., Roseman, A. M., Farr, G. W., Horwich, A. L., and Saibil, H. R. (2004) Nat. Struct. Mol. Biol. 11, 1128-1133
55. Guagliardi, A., Cerchia, L., Bartolucci, S., and Rossi, M. (1994) Protein Sci. 3, 1436-1443
56. Dobrzynski, J. K., Sternlicht, M. L., Farr, G. W., and Sternlicht, H. (1996) Biochemistry 35, 15870-15882
57. Spiess, C., Miller, E. J., McClellan, A. J., and Frydman, J. (2006) Mol. Cell 24, 25-37
58. Ranson, N. A., Clare, D. K., Farr, G. W., Houldershaw, D., Horwich, A. L., and Saibil, H. R. (2006) Nat. Struct. Mol. Biol. 13, 147-152