3e7x | pdb_00003e7x

Crystal structure of DLTA: implications for the reaction mechanism of non-ribosomal peptide synthetase (NRPS) adenylation domains

spinqualitylabelsall models 3e7x, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3e7x is a 1 chain structure with sequence from "vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: AMP Related: 1amu, 1md9, 2dls, 1ba3, 1pg4, 1hqb, 3e7w Gene: dltA ("Vibrio subtilis" Ehrenberg 1835) Activity: D-alanine--poly(phosphoribitol) ligase, with EC number 6.1.1.13 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [DLTA_BACSU] Involved in the biosynthesis of D-alanyl-lipoteichoic acid (LTA). Catalyzes an ATP-dependent two-step reaction where it forms a high energy D-alanyl AMP intermediate and transfers the alanyl residues from AMP to Dcp. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed DltA, the D-alanine:D-alanyl carrier protein ligase responsible for the initial step of lipoteichoic acid D-alanylation in Gram-positive bacteria, belongs to the adenylation domain superfamily, which also includes acetyl-CoA synthetase and the adenylation domains of non-ribosomal synthetases. The two-step reaction catalyzed by these enzymes (substrate adenylation followed by transfer to the reactive thiol group of CoA or the phosphopantheinyl prosthetic group of peptidyl carrier proteins) has been suggested to proceed via large scale rearrangements of structural domains within the enzyme. The structures of DltA reported here reveal the determinants for D-Ala substrate specificity and confirm that the peptidyl carrier protein-activating domains are able to adopt multiple conformational states, in this case corresponding to the thiolation reaction. Comparisons of available structures allow us to propose a mechanism whereby small perturbations of finely balanced metastable structural states would be able to direct an ordered formation of non-ribosomal synthetase products. Crystal structure of DltA. Implications for the reaction mechanism of non-ribosomal peptide synthetase adenylation domains.,Yonus H, Neumann P, Zimmermann S, May JJ, Marahiel MA, Stubbs MT J Biol Chem. 2008 Nov 21;283(47):32484-91. Epub 2008 Sep 10. PMID:18784082 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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