Crystal Structure of an Aldo-keto Reductase MGG_00097 from Magnaporthe grisea
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 catal...
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| Format: | Article |
| Language: | English |
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Hanrimwon Publishing Company
2025-04-01
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| Series: | The Plant Pathology Journal |
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| Online Access: | http://ppjonline.org/upload/pdf/PPJ-OA-07-2024-0115.pdf |
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| author | Xiaofang Huang Hui Jiang Yahong Lin Xiang Li Chuyun Bi Shiqian Qi Dan Tang Zonghua Wang Shiqiang Lin |
| author_facet | Xiaofang Huang Hui Jiang Yahong Lin Xiang Li Chuyun Bi Shiqian Qi Dan Tang Zonghua Wang Shiqiang Lin |
| author_sort | Xiaofang Huang |
| collection | DOAJ |
| description | 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. |
| format | Article |
| id | doaj-art-86d0fa0565d64e6e996f2f8be4d5e448 |
| institution | OA Journals |
| issn | 1598-2254 2093-9280 |
| language | English |
| publishDate | 2025-04-01 |
| publisher | Hanrimwon Publishing Company |
| record_format | Article |
| series | The Plant Pathology Journal |
| spelling | doaj-art-86d0fa0565d64e6e996f2f8be4d5e4482025-08-20T01:54:57ZengHanrimwon Publishing CompanyThe Plant Pathology Journal1598-22542093-92802025-04-0141216717810.5423/PPJ.OA.07.2024.01152498Crystal Structure of an Aldo-keto Reductase MGG_00097 from Magnaporthe griseaXiaofang Huang0Hui Jiang1Yahong Lin2Xiang Li3Chuyun Bi4Shiqian Qi5Dan Tang6Zonghua Wang7Shiqiang Lin8 Department of Urology, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University and Collaborative Innovation Center of Biotherapy, 610041 Chengdu, China Biobank of Pathology Department, Suining Central Hospital, 629000 Suining, China College of Life Science, Fujian Agriculture and Forestry University, 350002 Fuzhou, China Department of Urology, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University and Collaborative Innovation Center of Biotherapy, 610041 Chengdu, China Key Laboratory of Crop Biotechnology, Fujian Agriculture and Forestry University, Fujian Province Universities, 350002 Fuzhou, China Biobank of Pathology Department, Suining Central Hospital, 629000 Suining, China Department of Urology, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University and Collaborative Innovation Center of Biotherapy, 610041 Chengdu, China College of Life Science, Fujian Agriculture and Forestry University, 350002 Fuzhou, China Key Laboratory of Crop Biotechnology, Fujian Agriculture and Forestry University, Fujian Province Universities, 350002 Fuzhou, ChinaThe 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.http://ppjonline.org/upload/pdf/PPJ-OA-07-2024-0115.pdfaldo-keto reductasescrystal structuremgg_00097 |
| spellingShingle | Xiaofang Huang Hui Jiang Yahong Lin Xiang Li Chuyun Bi Shiqian Qi Dan Tang Zonghua Wang Shiqiang Lin Crystal Structure of an Aldo-keto Reductase MGG_00097 from Magnaporthe grisea The Plant Pathology Journal aldo-keto reductases crystal structure mgg_00097 |
| title | Crystal Structure of an Aldo-keto Reductase MGG_00097 from Magnaporthe grisea |
| title_full | Crystal Structure of an Aldo-keto Reductase MGG_00097 from Magnaporthe grisea |
| title_fullStr | Crystal Structure of an Aldo-keto Reductase MGG_00097 from Magnaporthe grisea |
| title_full_unstemmed | Crystal Structure of an Aldo-keto Reductase MGG_00097 from Magnaporthe grisea |
| title_short | Crystal Structure of an Aldo-keto Reductase MGG_00097 from Magnaporthe grisea |
| title_sort | crystal structure of an aldo keto reductase mgg 00097 from magnaporthe grisea |
| topic | aldo-keto reductases crystal structure mgg_00097 |
| url | http://ppjonline.org/upload/pdf/PPJ-OA-07-2024-0115.pdf |
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