BAIT

MXR1

msrA, L000004794, YER042W
Methionine-S-sulfoxide reductase; involved in the response to oxidative stress; protects iron-sulfur clusters from oxidative inactivation along with MXR2; involved in the regulation of lifespan; reduced activity of human homolog implicated in Alzheimer disease
GO Process (1)
GO Function (1)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)
PREY

MXR1

msrA, L000004794, YER042W
Methionine-S-sulfoxide reductase; involved in the response to oxidative stress; protects iron-sulfur clusters from oxidative inactivation along with MXR2; involved in the regulation of lifespan; reduced activity of human homolog implicated in Alzheimer disease
GO Process (1)
GO Function (1)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)

Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Publication

Structural plasticity of the thioredoxin recognition site of yeast methionine-S-sulfoxide reductase Mxr1.

Ma XX, Guo PC, Shi WW, Luo M, Tan XF, Chen Y, Zhou CZ

The methionine-S-sulfoxide reductase MsrA catalyzes the reduction of methionine sulfoxide, a ubiquitous reaction depending on the thioredoxin system. To investigate interactions between MsrA and thioredoxin (Trx), we determined the crystal structures of yeast MsrA/Mxr1 in their reduced, oxidized and Trx2-complexed forms, at 2.03, 1.90 and 2.70 A, respectively. Comparative structure analysis revealed significant conformational changes of the three loops, which ... [more]

Unknown Feb. 23, 2011; 0(0); [Pubmed: 21345799]

Throughput

  • Low Throughput

Curated By

  • BioGRID