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
Author(s)
김화영이은혜[이은혜]이기택[이기택]곽근희박연승[박연승]이공주[이공주]황광연[황광연]
Keywords
STRUCTURAL-ANALYSIS; ESCHERICHIA-COLI; MECHANISM; PROTEIN; GLUTAREDOXIN; ENZYME
Issue Date
201506
Publisher
PUBLIC LIBRARY SCIENCE
Citation
PLOS ONE, v.10, no.6
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.
URI
http://hdl.handle.net/YU.REPOSITORY/31975http://dx.doi.org/10.1371/journal.pone.0131523
ISSN
1932-6203
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의과대학 > 생화학.분자생물학교실 > Articles
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