NMR solution structure of the oxidized form of MerP, a mercuric ion binding protein involved in bacterial mercuric ion resistance

Biochemistry

Volumn 37, Issue 26, 1998, Pages 9316-9322

  Qian, Hong ^a   Sahlman, Lena ^a,d   Eriksson, Per Olof ^b   Hambraeus, Charlotta ^c   Edlund, Ulf ^a   Sethson, Ingmar ^a  

^a UMEÅ UNIVERSITY   (Sweden)

^b ASTRAZENECA R AND D   (Sweden)

^c SÖDERTÖRN UNIVERSITY   (Sweden)

^d Gina Cody School of Engineering and Computer Science   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; MERCURY;

ARTICLE; BINDING AFFINITY; CHEMICAL STRUCTURE; METAL BINDING; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

BACTERIAL PROTEINS; CARRIER PROTEINS; CRYSTALLOGRAPHY, X-RAY; DRUG RESISTANCE, MICROBIAL; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; MERCURY; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; OXIDATION-REDUCTION; OXIDOREDUCTASES; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEINS; SOLUTIONS; SURFACE PROPERTIES;

BACTERIA (MICROORGANISMS);

EID: 0032580972     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9803628     Document Type: Article

References (26)

1. Sahlman, L., Wong, W., and Powlowski, J. (1997) J. Biol. Chem. 272, 29518-29526.
2. Sahlman, L., and Jonsson, B.-H. (1992) Eur. J. Biochem. 205, 375-381.
3. Sahlman, L., and Skärfstad, E. G. (1993) Biochem. Biophys. Res. Commun. 196, 583-588.
4. Eriksson, P. O., and Sahlman, L. (1993) J. Biomol. NMR 3, 613-626.
5. Richardson, J. (1981) Adv. Protein Chem. 34, 167-339.
6. Quiocho, F. A., and Ledvina, P. S. (1996) Mol. Microbiol. 20, 17-25.
7. Steele, R. A., and Opella, S. J. (1997) Biochemistry 36, 6885-6895.
8. Muhandiram, D. R., and Kay, L. E. (1994) J. Magn. Reson., Ser. B 103, 203-216.
9. Kay, L. E., Xu, G.-Y., Singer, A. U., Muhandiram, D. R., and Forman-Kay, J. D. (1993) J. Magn. Reson., Ser. B 101, 333-337.
10. Zhang et al. (1994) J. Biomol. NMR 4, 845.
11. Pascal, S. M., Muhandiram, D. R., Yamazaki, T., Forman-Kay, J. D., and Kay, L. E. (1994) J. Magn. Reson., Ser. B 103, 197-201.
12. Kay, L. E., and Bax, A. (1990) J. Magn. Reson. 86, 110-126.
13. Luginbühl, P., Szyperski, T., and Wüthrich, K. (1995) J. Magn. Reson., Ser. B 109, 229-233.
14. Spera, S., and Bax, A. (1991) J. Am. Chem. Soc. 113, 5490-5492.
15. Brünger, A. T (1996) X-PLOR Manual Version 3.843, Yale University, New Haven, CT.
16. Nilges, M., Gronenborn, A. M., Brünger, A. T., and Clore, G. M. (1988) Protein Eng. 2, 27-38.
17. Nilges, M. A. (1993) Proteins 17, 295-309.
18. Fletcher, C. M., Jones, D. N. M., Diamond, R., and Neuhaus, D. (1996) J. Biomol. NMR 8, 292-310.
19. Laskowski, R. A., MacArther, M. W., Moss, D. S., and Thornton, J. M. (1993) J. Appl. Crystallogr. 26, 283-291.
20. Kelly, L. A., Gardner, S. P., and Sutcliffe, M. J. (1996) Protein Eng. 9, 1063-1065.
21. Jeng, M.-F., Campbell, A. P., Begley, T., Holmgren, A., Case, D. A., Wright, P. E., and Dyson, H. J. (1994) Structure 2, 853-868.
22. Summers, A. O. (1986) Annu. Rev. Microbiol. 40, 607-634.
23. Bull, P. C., and Cox, D. W. (1994) Trends Genet. 10, 246-252.
24. Fox, B. S., and Walsh, C. T. (1983) Biochemistry 22, 4082-4088.
25. Gitschier, J., Moffat, B., Reilly, D., Wood, W. I., and Fairbrother, W. J. (1998) Nat. Struct. Biol. 5, 47-54.
26. Branden, C., and Tooze, J. (1991) Introduction to Protein Structure, Garland Publishing Inc., New York.