Insights into function, catalytic mechanism, and fold evolution of selenoprotein methionine sulfoxide reductase B1 through structural analysis

Journal of Biological Chemistry

Volumn 285, Issue 43, 2010, Pages 33315-33323

  Aachmann, Finn L ^a   Sal, Lena S ^a   Kim, Hwa Young ^b   Marino, Stefano M ^c   Gladyshev, Vadim N ^c   Dikiy, Alexander ^a  

^a NORWEGIAN UNIVERSITY OF SCIENCE AND TECHNOLOGY   (Norway)

^b Yeungnam University College of Medicine   (South Korea)

^c BRIGHAM AND WOMEN S HOSPITAL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ATOMIC LEVELS; CATALYTIC MECHANISMS; HETERONUCLEAR; HIGH RESOLUTION NMR SPECTROSCOPY; METHIONINE RESIDUES; METHIONINE SULFOXIDE; METHIONINE SULFOXIDE REDUCTASE; N-TERMINALS; NMR SIGNALS; PH DEPENDENCE; SELENOCYSTEINE; SELENOPROTEINS; SPECTRAL ASSIGNMENTS; STRUCTURAL MODELS; THREE-DIMENSIONAL STRUCTURE;

AMINO ACIDS; CATALYSIS; ENZYME ACTIVITY; GEL PERMEATION CHROMATOGRAPHY; MAMMALS; METAL IONS; MODEL STRUCTURES; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; QUANTUM CHEMISTRY;

STRUCTURAL ANALYSIS;

CYSTEINE; METHIONINE SULFONE; METHIONINE SULFOXIDE; METHIONINE SULFOXIDE REDUCTASE B; METHIONINE SULFOXIDE REDUCTASE B1; SELENOCYSTEINE; SELENOPROTEIN; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; BETA SHEET; CATALYSIS; ENZYME ACTIVITY; ENZYME BINDING; ENZYME STRUCTURE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN FOLDING; STRUCTURE ANALYSIS;

AMINO ACID SUBSTITUTION; ANIMALS; CATALYSIS; ENZYME INHIBITORS; HYDROGEN-ION CONCENTRATION; METHIONINE; METHIONINE SULFOXIDE REDUCTASES; MICE; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SELENOCYSTEINE; STRUCTURE-ACTIVITY RELATIONSHIP;

BACTERIA (MICROORGANISMS); EUKARYOTA; MAMMALIA;

EID: 77958471283     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.132308     Document Type: Article

References (37)

1. Weissbach, H., Etienne, F., Hoshi, T., Heinemann, S. H., Lowther, W. T., Matthews, B., St. John, G., Nathan, C., and Brot, N. (2002) Arch. Biochem. Biophys. 397, 172-178
2. Kim, H. Y., and Gladyshev, V. N. (2007) Biochem. J. 407, 321-329
3. Lin, Z., Johnson, L. C., Weissbach, H., Brot, N., Lively, M. O., and Lowther, W. T. (2007) Proc. Natl. Acad. Sci. U.S.A. 104, 9597-9602
4. Lee, B. C., Le, D. T., and Gladyshev, V. N. (2008) J. Biol. Chem. 283, 28361-28369
5. Lee, S. R., Bar-Noy, S., Kwon, J., Levine, R. L., Stadtman, T. C., and Rhee, S. G. (2000) Proc. Natl. Acad. Sci. U.S.A. 97, 2521-2526
6. Stadtman, T. C. (1996) Annu. Rev. Biochem. 65, 83-100
7. Kim, H. Y., and Gladyshev, V. N. (2004) Mol. Biol. Cell 15, 1055-1064
8. Lowther, W. T., Weissbach, H., Etienne, F., Brot, N., and Matthews, B. W. (2002) Nat. Struct. Biol. 9, 348-352
9. Kumar, R. A., Koc, A., Cerny, R. L., and Gladyshev, V. N. (2002) J. Biol. Chem. 277, 37527-37535
10. Olry, A., Boschi-Muller, S., and Branlant, G. (2004) Biochemistry 43, 11616-11622
11. Kim, H. Y., and Kim, J. R. (2008) Biochem. Biophys. Res. Commun. 371, 490-494
12. Lee, T. H., and Kim, H. Y. (2008) Arch. Biochem. Biophys. 478, 175-180
13. Kim, H. Y., and Gladyshev, V. N. (2005) PLoS Biol. 3, e375
14. Kim, Y. K., Shin, Y. J., Lee, W. H., Kim, H. Y., and Hwang, K. Y. (2009) Mol. Microbiol. 72, 699-709
15. Sal, L. S., Aachmann, F. L., Kim, H. Y., Gladyshev, V. N., and Dikiy, A. (2007) Biomol. NMR Assign. 1, 131-133
16. Keller, R. L. J. (2004) Optimizing the Process of Nuclear Magnetic Resonance Spectrum Analysis and Computer Aided Resonance Assignment, CANTINA Verlag, Zürich
17. Farrow, N. A., Muhandiram, R., Singer, A. U., Pascal, S. M., Kay, C. M., Gish, G., Shoelson, S. E., Pawson, T., Forman-Kay, J. D., and Kay, L. E. (1994) Biochemistry 33, 5984-6003
18. Kay, L. E., Torchia, D. A., and Bax, A. (1989) Biochemistry 28, 8972-8979
19. Güntert, P., Braun, W., and Wüthrich, K. (1991) J. Mol. Biol. 217, 517-530
20. Cornilescu, G., Delaglio, F., and Bax, A. (1999) J. Biomol. NMR 13, 289-302
21. Chantalat, L., Leroy, D., Filhol, O., Nueda, A., Benitez, M. J., Chambaz, E. M., Cochet, C., and Dideberg, O. (1999) EMBO J. 18, 2930-2940
22. Colonna-Cesari, F., Perahia, D., Karplus, M., Eklund, H., Brädén, C. I., and Tapia, O. (1986) J. Biol. Chem. 261, 15273-15280
23. Mechulam, Y., Schmitt, E., Maveyraud, L., Zelwer, C., Nureki, O., Yokoyama, S., Konno, M., and Blanquet, S. (1999) J. Mol. Biol. 294, 1287-1297
24. Case, D. A., Cheatham, T. E., 3rd, Darden, T., Gohlke, H., Luo, R., Merz, K. M., Jr., Onufriev, A., Simmerling, C., Wang, B., and Woods, R. J. (2005) J. Comput. Chem. 26, 1668-1688
25. Kryukov, G. V., Kumar, R. A., Koc, A., Sun, Z., and Gladyshev, V. N. (2002) Proc. Natl. Acad. Sci. U.S.A. 99, 4245-4250
26. Boschi-Muller, S., Olry, A., Antoine, M., and Branlant, G. (2005) Biochim. Biophys. Acta 1703, 231-238
27. Kornhaber, G. J., Snyder, D., Moseley, H. N., and Montelione, G. T. (2006) J. Biomol. NMR 34, 259-269
28. Kauffmann, B., Aubry, A., and Favier, F. (2005) Biochim. Biophys. Acta 1703, 249-260
29. Cheighton, T. E. (1996) Protein: Structure and Molecular Properties, 2nd Ed., W. H. Freeman and Company, New York
30. Neiers, F., Sonkaria, S., Olry, A., Boschi-Muller, S., and Branlant, G. (2007) J. Biol. Chem. 282, 32397-32405
31. Olry, A., Boschi-Muller, S., Yu, H., Burnel, D., and Branlant, G. (2005) Protein Sci. 14, 2828-2837
32. Deleted in proof
33. Li, H., Robertson, A. D., and Jensen, J. H. (2005) Proteins 61, 704-721
34. Baker, N. A., Sept, D., Joseph, S., Holst, M. J., and McCammon, J. A. (2001) Proc. Natl. Acad. Sci. U.S.A. 98, 10037-10041
35. DeLano, W. L. (2002) The PyMOL User's Manual, DeLano Scientific, San Carlos, CA
36. Ranaivoson, F. M., Neiers, F., Kauffmann, B., Boschi-Muller, S., Branlant, G., and Favier, F. (2009) J. Mol. Biol. 394, 83-93
37. Neiers, F., Kriznik, A., Boschi-Muller, S., and Branlant, G. (2004) J. Biol. Chem. 279, 42462-42468