4PVC

Crystal structure of yeast methylglyoxal/ isovaleraldehyde reductase Gre2

4PVC の概要

• エントリーDOI: 10.2210/pdb4pvc/pdb
• 関連するPDBエントリー: 4PVD
• 分子名称: NADPH-dependent methylglyoxal reductase GRE2 (2 entities in total)
• 機能のキーワード: rossmann fold, reductase, nadph binding, oxidoreductase
• 由来する生物種: Saccharomyces cerevisiae (yeast)
• 細胞内の位置: Cytoplasm : Q12068
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 76440.87

構造登録者

Guo, P.C.,Bao, Z.Z.,Li, W.F.,Zhou, C.Z. (登録日: 2014-03-17, 公開日: 2014-10-22, 最終更新日: 2023-11-08)

主引用文献

Guo, P.C.,Bao, Z.Z.,Ma, X.X.,Xia, Q.,Li, W.F.
Structural insights into the cofactor-assisted substrate recognition of yeast methylglyoxal/isovaleraldehyde reductase Gre2
Biochim.Biophys.Acta, 1844:1486-1492, 2014

PubMed Abstract: Saccharomyces cerevisiae Gre2 (EC1.1.1.283) serves as a versatile enzyme that catalyzes the stereoselective reduction of a broad range of substrates including aliphatic and aromatic ketones, diketones, as well as aldehydes, using NADPH as the cofactor. Here we present the crystal structures of Gre2 from S. cerevisiae in an apo-form at 2.00Å and NADPH-complexed form at 2.40Å resolution. Gre2 forms a homodimer, each subunit of which contains an N-terminal Rossmann-fold domain and a variable C-terminal domain, which participates in substrate recognition. The induced fit upon binding to the cofactor NADPH makes the two domains shift toward each other, producing an interdomain cleft that better fits the substrate. Computational simulation combined with site-directed mutagenesis and enzymatic activity analysis enabled us to define a potential substrate-binding pocket that determines the stringent substrate stereoselectivity for catalysis.

PubMed: 24879127
DOI: 10.1016/j.bbapap.2014.05.008

実験手法

X-RAY DIFFRACTION (2 Å)