4U66

Induced Dimer Structure of Methionine Sulfoxide Reductase U16C from Clostridium Oremlandii

Summary for 4U66

• Entry DOI: 10.2210/pdb4u66/pdb
• Descriptor: Peptide methionine sulfoxide reductase MsrA, SULFATE ION (3 entities in total)
• Functional Keywords: alpha/beta fold, peptide-methionine (s)-s-oxide reductase, oxidoreductase
• Biological source: Alkaliphilus oremlandii OhILAs
• Total number of polymer chains: 3
• Total formula weight: 71476.99

Authors

Hwang, K.Y.,Lee, E.H. (deposition date: 2014-07-28, release date: 2015-07-15, Last modification date: 2023-11-08)

Primary citation

Lee, E.H.,Lee, K.,Kwak, G.H.,Park, Y.S.,Lee, K.J.,Hwang, K.Y.,Kim, H.Y.
Evidence for the Dimerization-Mediated Catalysis of Methionine Sulfoxide Reductase A from Clostridium oremlandii
Plos One, 10:e0131523-e0131523, 2015

PubMed 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.

PubMed: 26107511
DOI: 10.1371/journal.pone.0131523

Experimental method

X-RAY DIFFRACTION (2.9 Å)