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Solution structure of a zinc-binding methionine sulfoxide reductase

Source organism: Methanothermobacter thermautotrophicus str. Delta H
Biochemical function: metal ion binding
Biological process: protein repair
Cellular component: cytoplasm

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EC 1.8.4.12: Peptide-methionine (R)-S-oxide reductase

Reaction catalysed:
Peptide-L-methionine + thioredoxin disulfide + H(2)O = peptide-L-methionine (R)-S-oxide + thioredoxin
Systematic name:
Peptide-methionine:thioredoxin-disulfide S-oxidoreductase (methionine (R)-S-oxide-forming)
Alternative Name(s):
  • Methionine S-oxide reductase
  • Methionine S-oxide reductase (R-form oxidizing)
  • Methionine sulfoxide reductase
  • Methionine sulfoxide reductase B
  • MsrB
  • PMRsr
  • PMSR
  • PilB
  • SelR
  • SelX
  • Selenoprotein R

GO terms

Sequence family

Pfam Protein family (Pfam)
PF01641
Domain description: SelR domain
Occurring in:
  1. Peptide methionine sulfoxide reductase MsrB
The deposited structure of PDB entry 2k8d contains 1 copy of Pfam domain PF01641 (SelR domain) in Peptide methionine sulfoxide reductase MsrB. Showing 1 copy in chain A.

InterPro InterPro annotations
IPR002579
Domain description: Peptide methionine sulphoxide reductase MrsB domain
Occurring in:
  1. Peptide methionine sulfoxide reductase MsrB
IPR011057
Domain description: Mss4-like superfamily
Occurring in:
  1. Peptide methionine sulfoxide reductase MsrB
IPR028427
Domain description: Peptide methionine sulfoxide reductase MsrB
Occurring in:
  1. Peptide methionine sulfoxide reductase MsrB

Structure domain

CATH CATH domain
2.170.150.20
Class: Mainly Beta
Architecture: Beta Complex
Topology: Metal Binding Protein, Guanine Nucleotide Exchange Factor; Chain A
Homology: Peptide methionine sulfoxide reductase.
Occurring in:
  1. Peptide methionine sulfoxide reductase MsrB
The deposited structure of PDB entry 2k8d contains 1 copy of CATH domain 2.170.150.20 (Metal Binding Protein, Guanine Nucleotide Exchange Factor; Chain A) in Peptide methionine sulfoxide reductase MsrB. Showing 1 copy in chain A.

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