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Literature summary for 1.8.4.11 extracted from

  • 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 (2015), PLoS ONE, 10, e0131523 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.8.4.11

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of dimeric MsrA to 2.9 A resolution, 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 Alkaliphilus oremlandii

Protein Variants

Protein Variants Comment Organism
E55A almost completely inactive, dimerization is hardly detectable Alkaliphilus oremlandii
E55D almost completely inactive, incapable of dimerization Alkaliphilus oremlandii

Organism

Organism UniProt Comment Textmining
Alkaliphilus oremlandii A8MI53
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Alkaliphilus oremlandii OhILAs A8MI53
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Subunits

Subunits Comment Organism
dimer and monomer. Monomeric CoMsrA dimerizes in the presence of its substrate methionine sulfoxide via an intermolecular disulfide bond between catalytic Cys16 residues. The dimeric MsrA is resolved by the reductant glutaredoxin Alkaliphilus oremlandii
monomer and dimer. monomeric CoMsrA dimerizes in the presence of its substrate methionine sulfoxide via an intermolecular disulfide bond between catalytic Cys16 residues. The dimeric MsrA is resolved by the reductant glutaredoxin Alkaliphilus oremlandii