8YP2

the crystal structure of inactive Magnaporthe grisea oxidoreductase in complex with NADP and Glycerol

8YP2 の概要

• エントリーDOI: 10.2210/pdb8yp2/pdb
• 関連するPDBエントリー: 8YP9
• 分子名称: NADP-dependent oxidoreductase domain-containing protein, GLYCEROL, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (4 entities in total)
• 機能のキーワード: magnaporthe oryzae; oxidoreductase; glycerol; turgor pressure, oxidoreductase
• 由来する生物種: Pyricularia grisea (Crabgrass-specific blast fungus, Magnaporthe grisea)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 114977.41

構造登録者

Huang, X.,Jiang, H.,Tang, D.,Lin, S. (登録日: 2024-03-15, 公開日: 2025-03-19, 最終更新日: 2025-04-23)

主引用文献

Huang, X.,Jiang, H.,Lin, Y.,Li, X.,Bi, C.,Qi, S.,Tang, D.,Wang, Z.,Lin, S.
Crystal Structure of an Aldo-keto Reductase MGG_00097 from Magnaporthe grisea.
Plant Pathol J, 41:167-178, 2025

PubMed Abstract: The enzyme MGG_00097 from rice blast fungus (Magnaporthe grisea) is a NADPH-dependent oxidoreductase, involved in synthesizing glycerol from dihydroxyacetone phosphate and dihydroxyacetone. The 35.5-kDa monomer belongs to the aldo-keto reductase superfamily, characterized by a highly conserved catalytic tetrad. This study, elucidates the expression, purification, and kinetic properties of recombinant MGG_00097. The ternary complex of MGG_00097 with NADP+ and glycerol was refined to a 2.9 Å resolution, revealing critical insights into substrate binding and catalysis. NADP+ binds within the active site, with residues Ser221, Leu223, Ser225, Lys271, Ser272, Ser273, Thr274, Arg277, and Asn281 forming the substrate and cofactor-binding pockets. A Y56A mutation reveals the open conformation of the cofactor-binding pocket, with Glu29 and Gln226 functioning as hinge residues for the conformational changes upon cofactor binding. These findings contribute to the understanding of MGG_00097's catalytic mechanism and offer a basis for further biochemical and potential biotechnological applications.

PubMed: 40211621
DOI: 10.5423/PPJ.OA.07.2024.0115

実験手法

X-RAY DIFFRACTION (2.91 Å)