4etw

Structure of the Enzyme-ACP Substrate Gatekeeper Complex Required for Biotin Synthesis

spinqualitylabelsall models 4etw, resolution 2.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4etw is a 4 chain structure with sequence from "shigella_paradysenteriae"_weldin_1927 "shigella paradysenteriae" weldin 1927 and Shif8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ZMK Gene: bioH, SF3435, S4329 ("Shigella paradysenteriae" Weldin 1927), acpP, SFV_1114, SSON_1114 (SHIF8) Activity: [acyl-carrier_protein_methyl_ester_esterase Pimelyl-[acyl-carrier protein] methyl ester esterase], with EC number 3.1.1.85 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [BIOH_SHIFL] The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters.[HAMAP-Rule:MF_01260] [ACP_SHIF8] Carrier of the growing fatty acid chain in fatty acid biosynthesis.[HAMAP-Rule:MF_01217] Publication Abstract from PubMed Although the pimeloyl moiety was long known to be a biotin precursor, the mechanism of assembly of this C7 alpha,omega-dicarboxylic acid was only recently elucidated. In Escherichia coli, pimelate is made by bypassing the strict specificity of the fatty acid synthetic pathway. BioC methylates the free carboxyl of a malonyl thioester, which replaces the usual acetyl thioester primer. This atypical primer is transformed to pimeloyl-acyl carrier protein (ACP) methyl ester by two cycles of fatty acid synthesis. The question is, what stops this product from undergoing further elongation? Although BioH readily cleaves this product in vitro, the enzyme is nonspecific, which made assignment of its physiological substrate problematical, especially because another enzyme, BioF, could also perform this gatekeeping function. We report the 2.05-A resolution cocrystal structure of a complex of BioH with pimeloyl-ACP methyl ester and use the structure to demonstrate that BioH is the gatekeeper and its physiological substrate is pimeloyl-ACP methyl ester. Structure of the enzyme-acyl carrier protein (ACP) substrate gatekeeper complex required for biotin synthesis.,Agarwal V, Lin S, Lukk T, Nair SK, Cronan JE Proc Natl Acad Sci U S A. 2012 Oct 23;109(43):17406-11. doi:, 10.1073/pnas.1207028109. Epub 2012 Oct 8. PMID:23045647 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Acyl carrier protein 3D structures Beta-ketoacyl carrier protein reductase 3D structures

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