Evidence map›Paper›PMID 40211621›Full record

ArticleThe plant pathology journal2025

Crystal Structure of an Aldo-keto Reductase MGG_00097 from Magnaporthe grisea.

Xiaofang Huang, Hui Jiang, Yahong Lin, Xiang Li, Chuyun Bi, Shiqian Qi, Dan Tang, Zonghua Wang, Shiqiang Lin

Abstract read
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In one paragraph

Article in The plant pathology journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

9 authors.

Xiaofang HuangDepartment of Urology, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University and Collaborative Innovation Center of Biotherapy, 610041 Chengdu, China.
Hui JiangBiobank of Pathology Department, Suining Central Hospital, 629000 Suining, China.
Yahong LinCollege ofLife Science, Fujian Agriculture and Forestry University, 350002 Fuzhou, China.
Xiang LiDepartment of Urology, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University and Collaborative Innovation Center of Biotherapy, 610041 Chengdu, China.
Chuyun BiKey Laboratory of Crop Biotechnology, Fujian Agriculture and Forestry University, Fujian Province Universities, 350002 Fuzhou, China.
Shiqian QiBiobank of Pathology Department, Suining Central Hospital, 629000 Suining, China.
Dan TangDepartment of Urology, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University and Collaborative Innovation Center of Biotherapy, 610041 Chengdu, China.
Zonghua WangCollege ofLife Science, Fujian Agriculture and Forestry University, 350002 Fuzhou, China.
Shiqiang LinKey Laboratory of Crop Biotechnology, Fujian Agriculture and Forestry University, Fujian Province Universities, 350002 Fuzhou, China.

Funding

National Natural Science Foundation of China 32201025
6 · The paper itself

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.

Indexed as

aldo-keto reductasescrystal structureMagnaporthe griseaMGG_00097

Identifiers

PMID40211621
PMCPMC11986364

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.