Structure of the ubiquitin-activating enzyme loaded with two ubiquitin molecules

Acta Crystallographica Section D: Biological Crystallography

Volumn 70, Issue 5, 2014, Pages 1311-1320

  Schäfer, Antje ^a   Kuhn, Monika ^a   Schindelin, Hermann ^a  

^a UNIVERSITY OF WÜRZBURG   (Germany)

Author keywords

acyladenylate; Uba1; ubiquitin; ubiquitin thioester; ubiquitin activating enzyme (E1)

Indexed keywords

CYSTEINE; SACCHAROMYCES CEREVISIAE PROTEIN; UBIQUITIN; UBIQUITIN PROTEIN LIGASE;

CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVE SITE; METABOLISM; PROTEIN TERTIARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; CYSTEINE; MODELS, MOLECULAR; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE PROTEINS; UBIQUITIN; UBIQUITIN-ACTIVATING ENZYMES;

EID: 84900439199     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S1399004714002910     Document Type: Article

References (35)

1. Adams, P. D. et al. (2010). Acta Cryst. D66, 213-221.
2. Burroughs, A. M., Iyer, L. M. & Aravind, L. (2009). Proteins, 75, 895-910.
3. Burroughs, A. M., Iyer, L. M. & Aravind, L. (2012). Methods Mol. Biol. 832, 15-63.
4. Ciechanover, A., Heller, H., Katz-Etzion, R. & Hershko, A. (1981). Proc. Natl Acad. Sci. USA, 78, 761-765.
5. Duda, D. M., Walden, H., Sfondouris, J. & Schulman, B. A. (2005). J. Mol. Biol. 349, 774-786.
6. Emsley, P. & Cowtan, K. (2004). Acta Cryst. D60, 2126-2132.
7. Evans, P. (2006). Acta Cryst. D62, 72-82.
8. Goldberg, A. L. (2007). Biochem. Soc. Trans. 35, 12-17.
9. Haas, A. L. & Rose, I. A. (1982). J. Biol. Chem. 257, 10329-10337.
10. Haas, A. L., Warms, J. V., Hershko, A. & Rose, I. A. (1982). J. Biol. Chem. 257, 2543-2548.
11. Haas, A. L., Warms, J. V. & Rose, I. A. (1983). Biochemistry, 22, 4388-4394.
12. Hänzelmann, P., Schäfer, A., Völler, D. & Schindelin, H. (2012). Methods Mol. Biol. 832, 547-576.
13. Huang, D. T., Hunt, H. W., Zhuang, M., Ohi, M. D., Holton, J. M. & Schulman, B. A. (2007). Nature (London), 445, 394-398.
14. Kabsch, W. (1976). Acta Cryst. A32, 922-923.
15. Kabsch, W. (1978). Acta Cryst. A34, 827-828.
16. Kabsch, W. (2010). Acta Cryst. D66, 125-132.
17. Kim, R., Yokota, H. & Kim, S.-H. (2000). Anal. Biochem. 282, 147-149.
18. Krissinel, E. & Henrick, K. (2004). Acta Cryst. D60, 2256-2268.
19. Krissinel, E. & Henrick, K. (2007). J. Mol. Biol. 372, 774-797.
20. Lake, M. W., Wuebbens, M. M., Rajagopalan, K. V. & Schindelin, H. (2001). Nature (London), 414, 325-329.
21. Lee, I. & Schindelin, H. (2008). Cell, 134, 268-278.
22. Lehmann, C., Begley, T. P. & Ealick, S. E. (2006). Biochemistry, 45, 11-19.
23. Lois, L. M. & Lima, C. D. (2005). EMBO J. 24, 439-451.
24. McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C. & Read, R. J. (2007). J. Appl. Cryst. 40, 658-674.
25. Metzger, M. B., Hristova, V. A. &Weissman, A. M. (2012). J. Cell Sci. 125, 531-537.
26. Olsen, S. K., Capili, A. D., Lu, X., Tan, D. S. & Lima, C. D. (2010). Nature (London), 463, 906-912.
27. Olsen, S. K. & Lima, C. D. (2013). Mol. Cell, 49, 884-896.
28. Petroski, M. D. (2008). BMC Biochem. 9, S7.
29. Pickart, C. M. & Rose, I. A. (1985). Prog. Clin. Biol. Res. 180, 215.
30. Rajagopalan, K. V. (1997). Biochem. Soc. Trans. 25, 757-761.
31. Reinstein, E. & Ciechanover, A. (2006). Ann. Intern. Med. 145, 676-684.
32. Rudolph, M. J., Wuebbens, M. M., Rajagopalan, K. V. & Schindelin, H. (2001). Nature Struct. Biol. 8, 42-46.
33. Schulman, B. A. & Harper, J. W. (2009). Nature Rev. Mol. Cell Biol. 10, 319-331.
34. Veen, A. G. van der & Ploegh, H. L. (2012). Annu. Rev. Biochem. 81, 323-357.
35. Walden, H., Podgorski, M. S., Huang, D. T., Miller, D. W., Howard, R. J., Minor, D. L. Jr, Holton, J. M. & Schulman, B. A. (2003). Mol. Cell, 12, 1427-1437.