Format

Send to

Choose Destination
See comment in PubMed Commons below
Biochim Biophys Acta. 2005 Jan 17;1703(2):249-60.

The three-dimensional structures of peptide methionine sulfoxide reductases: current knowledge and open questions.

Author information

1
Laboratoire de Cristallographie et de Modélisation des Matériaux Minéraux et Biologiques, UMR CNRS-UHP 7036, Université Henri Poincaré, BP 239, 54506 Vandoeuvre, France.

Abstract

Methionine sulfoxides are easily formed in proteins exposed to reactive oxidative species commonly present in cells. Their reduction back to methionine residues is catalyzed by peptide methionine sulfoxide reductases. Although grouped in a unique family with respect to their biological function, these enzymes are divided in two classes named MsrA and MsrB, depending on the sulfoxide enantiomer of the substrate they reduce. This specificity-based classification differentiates enzymes which display no sequence homology. Several three-dimensional structures of peptide methionine sulfoxide reductases have been determined, so that members of both classes are known to date. These crystal structures are reviewed in this paper. The folds and active sites of MsrAs and MsrBs are discussed in the light of the methionine sulfoxide reductase sequence diversity.

PMID:
15680233
DOI:
10.1016/j.bbapap.2004.09.008
[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science
    Loading ...
    Support Center