Crystal structures of the organomercurial lyase MerB in its free and mercury-bound forms Insights into the mechanism of methylmercury degradation

Journal of Biological Chemistry

Volumn 284, Issue 2, 2009, Pages 938-944

  Lafrance Vanasse, Julien ^a   Lefebvre, Maryse ^a   Lello, Paola Di ^a   Sygusch, Jurgen ^a   Omichinski, James G ^a  

^a UNIVERSITÉ DE MONTRÉAL   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

AMINATION; AMINES; MERCURY (METAL); MERCURY COMPOUNDS; NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; ORGANIC ACIDS; PORT TERMINALS; PROTON TRANSFER;

ACTIVE SITES; ASPARTIC ACIDS; BACTERIA RESISTANTS; BOND CLEAVAGES; CATALYTIC SITES; CORE REGIONS; ELEMENTAL MERCURIES; HIGH RESOLUTION CRYSTAL STRUCTURES; IONIC MERCURIES; METHYL MERCURIES; NMR STRUCTURES; SUBSTRATE BINDINGS;

CRYSTAL STRUCTURE;

ASPARTIC ACID; BACTERIAL ENZYME; CARBON; CYSTEINE; MERCURY; ORGANOMERCURIAL LYASE MERB; RECOMBINANT ENZYME; UNCLASSIFIED DRUG;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; ENZYMATIC DEGRADATION; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME BINDING; METAL BINDING; NUCLEAR MAGNETIC RESONANCE IMAGING; PRIORITY JOURNAL; PROTEIN CLEAVAGE; PROTEIN PROTEIN INTERACTION; PROTON TRANSPORT; STRUCTURAL PROTEOMICS; STRUCTURE ANALYSIS;

BACTERIAL PROTEINS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; CYSTEINE; ESCHERICHIA COLI; LYASES; METHYLMERCURY COMPOUNDS; MODELS, MOLECULAR; MUTATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY;

EID: 59449093704     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M807143200     Document Type: Article

References (37)

1. Clarkson, T. W., and Magos, L. (2006) Crit. Rev. Toxicol. 36, 609-662
2. Mergler, D., Anderson, H. A., Chan, L. H., Mahaffey, K. R., Murray, M., Sakamoto, M., and Stern, A. H. (2007) Ambio 36, 3-11
3. Scheuhammer, A. M., Meyer, M. W., Sandheinrich, M. B., and Murray, M. W. (2007) Ambio 36, 12-18
4. Moore, B. (1960) Lancet 2, 453-458
5. Richmond, M. H., and John, M. (1964) Nature 202, 1360-1361
6. Novick, R. P., and Roth, C. (1968) J. Bacteriol. 95, 1335-1342
7. Summers, A. O. (1986) Annu. Rev. Microbiol. 40, 607-634
8. Schottel, J. L. (1978) J. Biol. Chem. 253, 4341-4349
9. Summers, A. O., and Sugarman, L. I. (1974) J. Bacteriol. 119, 242-249
10. Lyyra, S., Meagher, R. B., Kim, T., Heaton, A., Montello, P., Balish, R. S., and Merkle, S. A. (2007) Plant Biotechnol. J. 5, 254-262
11. Che, D., Meagher, R. B., Rugh, C. L., Kim, T., Heaton, A. C. P., and Merkle, S. A. (2006) In Vitro Cell Dev. Biol. Plant 42, 228-234
12. Bizily, S. P., Rugh, C. L., and Meagher, R. B. (2000) Nat. Biotechnol. 18, 213-217
13. Bizily, S. P., Rugh, C. L., Summers, A. O., and Meagher, R. B. (1999) Proc. Natl Acad Sci U S A 96, 6808-6813
14. Begley, T. P., Walts, A. E., and Walsh, C. T. (1986) Biochemistry 25, 7186-7192
15. Begley, T. P., Walts, A. E., and Walsh, C. T. (1986) Biochemistry 25, 7192-7200
16. Pitts, K. E., and Summers, A. O. (2002) Biochemistry 41, 10287-10296
17. Di Lello, P., Benison, G. C., Valafar, H., Pitts, K. E., Summers, A. O., Legault, P., and Omichinski, J. G. (2004) Biochemistry 43, 8322-8332
18. Melnick, J. G., and Parkin, G. (2007) Science 317, 225-227
19. Otwinowski, Z., and Minor, W. (1997) Methods Enzymol. 276, 307-326
20. Terwilliger, T. C., and Berendzen, J. (1999) Acta Crystallogr. Sect. D Biol. Crystallogr. 55, 849-861
21. Terwilliger, T. C. (2000) Acta Crystallogr. Sect. D Biol. Crystallogr. 56, 965-972
22. Terwilliger, T. C. (2003) Acta Crystallogr. Sect. D Biol. Crystallogr. 59, 38-44
23. Perrakis, A., Morris, R., and Lamzin, V. S. (1999) Nat. Struct. Biol. 6, 458-463
24. Brunger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J.-S., Kuszewski, J., Nilges, M., Pannu, N. S., Read, R. J., Rice, L. M., Simonson, T., and Warren, G. L. (1998) Acta Crystallogr. Sect. D Biol. Crystallogr. 54, 905-921
25. 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. Sect. D Biol. Crystallogr. 58, 1948-1954
26. Afonine, P. V., Grosse-Kunstleve, R. W., and Adams, P. D. (2005) in CCP4 Newsletter 42, Daresbury Laboratory, Warrington, UK
27. Emsley, P., and Cowtan, K. (2004) Acta Crystallogr. Sect. D Biol. Crystallogr. 60, 2126-2132
28. Davis, I. W., Leaver-Fay, A., Chen, V. B., Block, J. N., Kapral, G. J., Wang, X., Murray, L. W., Arendall, W. B., III, Snoeyink, J., Richardson, J. S., and Richardson, D. C. (2007) Nucleic Acids Res. 35, W375-W383
29. DeLano, W. L. (2002) The PyMOL Molecular Graphics System, DeLano Scientific LLC, San Carlos, CA
30. Richards, F. M., and Kundrot, C. E. (1988) Proteins 3, 71-84
31. Holm, L., and Sander, C. (1996) Science 273, 595-603
32. Taubner, L. M., McGuirl, M. A., Dooley, D. M., and Copie, V. (2006) Biochemistry 45, 12240-12252
33. Holm, L., and Park, J. (2000) Bioinformatics 16, 566-567
34. Benison, G. C., Di Lello, P., Shokes, J. E., Cosper, N. J., Scott, R. A., Legault, P., and Omichinski, J. G. (2004) Biochemistry 43, 8333-8345
35. Wilhelm, M., Deeken, S., Berssen, E., Saak, W., Lützen, A., Koch, R., and Strasdeit, H. (2004) Eur. J. Inorg. Chem. 2004, 2301-2312
36. Huang, C. C., Narita, M., Yamagata, T., and Endo, G. (1999) Gene (Amst.) 239, 361-366
37. Gopinath, E., and Bruice, T. C. (1987) J.Am. Chem. Soc. 109, 7903-7905