Kauffmann Brice, Aubry André, Favier Frédérique
Laboratoire de Cristallographie et de Modélisation des Matériaux Minéraux et Biologiques, UMR CNRS-UHP 7036, Université Henri Poincaré, BP 239, 54506 Vandoeuvre, France.
Biochim Biophys Acta. 2005 Jan 17;1703(2):249-60. doi: 10.1016/j.bbapap.2004.09.008.
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.
蛋氨酸亚砜很容易在暴露于细胞中常见的活性氧化物质的蛋白质中形成。它们还原为蛋氨酸残基的过程由肽甲硫氨酸亚砜还原酶催化。尽管就其生物学功能而言，这些酶归为一个独特的家族，但根据它们所还原底物的亚砜对映体，这些酶被分为两类，即MsrA和MsrB。这种基于特异性的分类区分了没有序列同源性的酶。肽甲硫氨酸亚砜还原酶的几个三维结构已被确定，因此到目前为止，两类酶的成员都已为人所知。本文对这些晶体结构进行了综述。根据甲硫氨酸亚砜还原酶序列的多样性，讨论了MsrA和MsrB的折叠和活性位点。
