8YP9

the crystal structure of wildtype Magnaporthe grisea oxidoreductase in complex with NADP

Summary for 8YP9

• Entry DOI: 10.2210/pdb8yp9/pdb
• Related: 8YP2
• Descriptor: NADP-dependent oxidoreductase domain-containing protein, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• Functional Keywords: magnaporthe oryzae; oxidoreductase; glycerol; turgor pressure, oxidoreductase
• Biological source: Pyricularia grisea (Crabgrass-specific blast fungus, Magnaporthe grisea)
• Total number of polymer chains: 3
• Total formula weight: 114977.41

Authors

Huang, X.,Jiang, H.,Tang, D.,Lin, S. (deposition date: 2024-03-15, release date: 2025-03-19, Last modification date: 2025-04-23)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.3 Å)