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      저자 : Del Conte, Rebecca (검색결과 1 건)
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        Structural and biochemical analysis of mammalian methionine sulfoxide reductase B2

        Aachmann, Finn L.,Kwak, Geun‐,Hee,Del Conte, Rebecca,Kim, Hwa‐,Young,Gladyshev, Vadim N.,Dikiy, Alexander Wiley Subscription Services, Inc., A Wiley Company 2011 Proteins Vol.79 No.11

        <P><B>Abstract</B></P><P>Methionine sulfoxide reductases are antioxidant enzymes that repair oxidatively damaged methionine residues in proteins. Mammals have three members of the methionine‐R‐sulfoxide reductase family, including cytosolic MsrB1, mitochondrial MsrB2, and endoplasmic reticulum MsrB3. Here, we report the solution structure of reduced Mus musculus MsrB2 using high resolution nuclear magnetic resonance (NMR) spectroscopy. MsrB2 is a β‐strand rich globular protein consisting of eight antiparallel β‐strands and three N‐terminal α‐helical segments. The latter secondary structure elements represent the main structural difference between mammalian MsrB2 and MsrB1. Structural comparison of mammalian and bacterial MsrB structures indicates that the general topology of this MsrB family is maintained and that MsrB2 more resembles bacterial MsrBs than MsrB1. Structural and biochemical analysis supports the catalytic mechanism of MsrB2 that, in contrast to MsrB1, does not involve a resolving cysteine (Cys). pH dependence of catalytically relevant residues in MsrB2 was accessed by NMR spectroscopy and the p<I>K</I><SUB>a</SUB> of the catalytic Cys162 was determined to be 8.3. In addition, the pH‐dependence of MsrB2 activity showed a maximum at pH 9.0, suggesting that deprotonation of the catalytic Cys is a critical step for the reaction. Further mobility analysis showed a well‐structured N‐terminal region, which contrasted with the high flexibility of this region in MsrB1. Our study highlights important structural and functional aspects of mammalian MsrB2 and provides a unifying picture for structure‐function relationships within the MsrB protein family. Proteins 2011; © 2011 Wiley‐Liss, Inc.</P>

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