4b4w

Crystal structure of Acinetobacter baumannii N5, N10- methylenetetrahydrofolate dehydrogenase-cyclohydrolase (FolD) complexed with NADP cofactor and an inhibitor

spinqualitylabelsall models 4b4w, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4b4w is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 9L9, CL, GOL, NAP Related: 4b4u, 4b4v Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [D0CBC8_ACIBA] Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.[HAMAP-Rule:MF_01576][SAAS:SAAS00020424] Publication Abstract from PubMed The bifunctional N(5) , N(10) methylenetetrahydrofolate dehydrogenase/cyclohydrolase (DHCH or FolD), widely distributed in prokaryotes and eukaryotes, is involved in biosynthesis of folate cofactors essential for growth and cellular development. The enzyme activities represent a potential antimicrobial drug target. We have characterized the kinetic properties of FolD from the Gram-negative pathogen Acinetobacter baumanni and determined high-resolution crystal structures of complexes with cofactor and two potent inhibitors. The data reveal new details with respect to the molecular basis of catalysis and potent inhibition. A major surprise was that our crystallographic data revealed a different structure for LY374571, an inhibitor studied as an antifolate, that was previously published. The implications of this observation are discussed. (c) 2012 The Authors Journal compilation (c) 2012 FEBS. Acinetobacter baumannii FolD ligand complexes; potent inhibitors of folate metabolism and a re-evaluation of the LY374571 structure.,Eadsforth TC, Maluf FV, Hunter WN FEBS J. 2012 Oct 10. doi: 10.1111/febs.12025. PMID:23050773 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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