5vcb

Crystal structure of holo-(acyl-carrier-protein) synthase:holo(acyl-carrier-protein) complex from Escherichia Coli.

spinqualitylabelsall models 5vcb, resolution 4.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5vcb is a 30 chain structure with sequence from Eco45 and Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PNS Gene: acpS, dpj, b2563, JW2547 (ECOLI), acpP, ECS88_1108 (ECO45) Activity: [acyl-carrier-protein_synthase Holo-[acyl-carrier-protein] synthase], with EC number 2.7.8.7 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ACPS_ECOLI] Transfers the 4'-phosphopantetheine moiety from coenzyme A to the 'Ser-36' of acyl-carrier-protein. [ACP_ECO45] Carrier of the growing fatty acid chain in fatty acid biosynthesis.[HAMAP-Rule:MF_01217] Publication Abstract from PubMed The Escherichia coli holo-(acyl carrier protein) synthase (ACPS) catalyzes the coenzyme A-dependent activation of apo-ACPP to generate holo-(acyl carrier protein) (holo-ACPP) in an early step of fatty acid biosynthesis. E. coli ACPS is sufficiently different from the human fatty acid synthase to justify the development of novel ACPS-targeting antibiotics. Models of E. coli ACPS in unliganded and holo-ACPP-bound forms solved by X-ray crystallography to 2.05A and 4.10A, respectively, revealed ACPS bound three product holo-ACPP molecules to form a 3:3 hexamer. Solution NMR spectroscopy experiments validated the ACPS binding interface on holo-ACPP using chemical shift perturbations and by determining the relative orientation of holo-ACPP to ACPS by fitting residual dipolar couplings. The binding interface is organized to arrange contacts between positively charged ACPS residues and the holo-ACPP phosphopantetheine moiety, indicating product contains more stabilizing interactions than expected in the enzyme:substrate complex. Indeed, holo-ACPP bound the enzyme with greater affinity than the substrate, apo-ACPP, and with negative cooperativity. The first equivalent of holo-ACPP bound with a KD=62+/-13nM, followed by the binding of two more equivalents of holo-ACPP with KD=1.2+/-0.2muM. Cooperativity was not observed for apo-ACPP which bound with KD=2.4+/-0.1muM. Strong product binding and high levels of holo-ACPP in the cell identify a potential regulatory role of ACPS in fatty acid biosynthesis. Structure, high affinity and negative cooperativity of the Escherichia coli holo-(acyl carrier protein):holo-(acyl carrier protein) synthase complex.,Marcella AM, Culbertson SJ, Shogren-Knaak MA, Barb AW J Mol Biol. 2017 Oct 17. pii: S0022-2836(17)30497-7. doi:, 10.1016/j.jmb.2017.10.015. PMID:29054754 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Acyl carrier protein 3D structures Acyl carrier protein synthase 3D structures

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