3ZU2

Structure of the enoyl-ACP reductase FabV from Yersinia pestis with the cofactor NADH (SIRAS)

Summary for 3ZU2

• Entry DOI: 10.2210/pdb3zu2/pdb
• Related: 3ZU3 3ZU4 3ZU5
• Descriptor: PUTATIVE REDUCTASE YPO4104/Y4119/YP_4011, 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE, SODIUM ION, ... (4 entities in total)
• Functional Keywords: oxidoreductase, fatty acid biosynthesis ii, short-chain dehydrogenase reductase superfamily
• Biological source: YERSINIA PESTIS
• Total number of polymer chains: 1
• Total formula weight: 46610.14

Authors

Hirschbeck, M.W.,Kuper, J.,Kisker, C. (deposition date: 2011-07-13, release date: 2012-01-18, Last modification date: 2024-05-08)

Primary citation

Hirschbeck, 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

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

Experimental method

X-RAY DIFFRACTION (2.1 Å)