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3ZU5

Structure of the enoyl-ACP reductase FabV from Yersinia pestis with the cofactor NADH and the 2-pyridone inhibitor PT173

Summary for 3ZU5
Entry DOI10.2210/pdb3zu5/pdb
Related3ZU2 3ZU3 3ZU4
DescriptorPUTATIVE REDUCTASE YPO4104/Y4119/YP_4011, 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE, 1-(3-amino-2-methylbenzyl)-4-hexylpyridin-2(1H)-one, ... (5 entities in total)
Functional Keywordsoxidoreductase, fatty acid biosynthesis ii, short-chain dehydrogenase reductase superfamily, structure-based drug design
Biological sourceYERSINIA PESTIS
Total number of polymer chains1
Total formula weight45019.47
Authors
Hirschbeck, M.W.,Kuper, J.,Tonge, P.J.,Kisker, C. (deposition date: 2011-07-13, release date: 2012-01-18, Last modification date: 2024-05-08)
Primary citationHirschbeck, M.W.,Kuper, J.,Lu, H.,Liu, N.,Neckles, C.,Shah, S.,Wagner, S.,Sotriffer, C.A.,Tonge, P.J.,Kisker, C.
Structure of the Yersinia Pestis Fabv Enoyl-Acp Reductase and its Interaction with Two 2-Pyridone Inhibitors
Structure, 20:89-, 2012
Cited by
PubMed Abstract: The recently discovered FabV enoyl-ACP reductase, which catalyzes the last step of the bacterial fatty acid biosynthesis (FAS-II) pathway, is a promising but unexploited drug target against the reemerging pathogen Yersinia pestis. The structure of Y. pestis FabV in complex with its cofactor reveals that the enzyme features the common architecture of the short-chain dehydrogenase reductase superfamily, but contains additional structural elements that are mostly folded around the usually flexible substrate-binding loop, thereby stabilizing it in a very tight conformation that seals the active site. The structures of FabV in complex with NADH and two newly developed 2-pyridone inhibitors provide insights for the development of new lead compounds, and suggest a mechanism by which the substrate-binding loop opens to admit the inhibitor, a motion that could also be coupled to the interaction of FabV with the acyl-carrier protein substrate.
PubMed: 22244758
DOI: 10.1016/J.STR.2011.07.019
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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数据于2025-10-15公开中

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