3PIM

Crystal structure of Mxr1 from Saccharomyces cerevisiae in unusual oxidized form

3PIM の概要

• エントリーDOI: 10.2210/pdb3pim/pdb
• 関連するPDBエントリー: 3PIL 3PIN
• 分子名称: Peptide methionine sulfoxide reductase (2 entities in total)
• 機能のキーワード: methionine-s-sulfoxide reductase, oxidoreductase
• 由来する生物種: Saccharomyces cerevisiae (yeast)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 64533.57

構造登録者

Ma, X.X.,Guo, P.C.,Shi, W.W.,Luo, M.,Tan, X.F.,Chen, Y.,Zhou, C.Z. (登録日: 2010-11-07, 公開日: 2011-02-23, 最終更新日: 2024-11-20)

主引用文献

Ma, X.X.,Guo, P.C.,Shi, W.W.,Luo, M.,Tan, X.F.,Chen, Y.,Zhou, C.Z.
Structural plasticity of the thioredoxin recognition site of yeast methionine S-sulfoxide reductase Mxr1
J.Biol.Chem., 286:13430-13437, 2011

PubMed Abstract: 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 Å, respectively. Comparative structure analysis revealed significant conformational changes of the three loops, which form a plastic "cushion" to harbor the electron donor Trx2. The flexible C-terminal loop enabled Mxr1 to access the methionine sulfoxide on various protein substrates. Moreover, the plasticity of the Trx binding site on Mxr1 provides structural insights into the recognition of diverse substrates by a universal catalytic motif of Trx.

PubMed: 21345799
DOI: 10.1074/jbc.M110.205161

実験手法

X-RAY DIFFRACTION (1.9 Å)