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Evidence for the dimerization-mediated catalysis of methionine sulfoxide reductase a from Clostridium oremlandii
- Title
- Evidence for the dimerization-mediated catalysis of methionine sulfoxide reductase a from Clostridium oremlandii
- Authors
- Lee E.H.; Lee K.; Kwak G.-H.; Park Y.S.; Lee K.-J.; Hwang K.Y.; Kim H.-Y.
- Ewha Authors
- 이공주
- SCOPUS Author ID
- 이공주
- Issue Date
- 2015
- Journal Title
- PLoS ONE
- ISSN
- 1932-6203
- Citation
- PLoS ONE vol. 10, no. 6
- Publisher
- Public Library of Science
- Indexed
- SCIE; SCOPUS
- Document Type
- Article
- Abstract
- Clostridium oremlandii MsrA (CoMsrA) is a natively selenocysteine-containing methionine-S-sulfoxide reductase and classified into a 1-Cys type MsrA. CoMsrA exists as a monomer in solution. Herein, we report evidence that CoMsrA can undergo homodimerization during catalysis. The monomeric CoMsrA dimerizes in the presence of its substrate methionine sulfoxide via an intermolecular disulfide bond between catalytic Cys16 residues. The dimeric CoMsrA is resolved by the reductant glutaredoxin, suggesting the relevance of dimerization in catalysis. The dimerization reaction occurs in a concentration- and time-dependent manner. In addition, the occurrence of homodimer formation in the native selenoprotein CoMsrA is confirmed. We also determine the crystal structure of the dimeric CoMsrA, having the dimer interface around the two catalytic Cys16 residues. A central cone-shaped hole is present in the surface model of dimeric structure, and the two Cys16 residues constitute the base of the hole. Collectively, our biochemical and structural analyses suggest a novel dimerization-mediated mechanism for CoMsrA catalysis that is additionally involved in CoMsrA regeneration by glutaredoxin. © 2015 Lee et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
- DOI
- 10.1371/journal.pone.0131523
- Appears in Collections:
- 약학대학 > 약학과 > Journal papers
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