4bpf | pdb_00004bpf

High resolution crystal structure of Bacillus subtilis DltC S36A

spinqualitylabelsall models 4bpf, resolution 1.01Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4bpf 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. NonStd Res: MSE Related: 4bpg, 4bph Activity: D-alanine--poly(phosphoribitol) ligase, with EC number 6.1.1.13 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [DLTC_BACSU] Involved in the biosynthesis of D-alanyl-lipoteichoic acid (LTA). Activated D-alanyl-Dcp donates its D-alanyl substituent to membrane-associated LTA. Publication Abstract from PubMed d-Alanylation of lipoteichoic acids plays an important role in modulating the properties of Gram-positive bacteria cell walls. The d-alanyl carrier protein DltC from Bacillus subtilis has been solved in apo- and two cofactor-modified holo-forms, whereby the entire phosphopantetheine moiety is defined in one. The atomic resolution of the apo-structure allows delineation of alternative conformations within the hydrophobic core of the 78 residue four helix bundle. In contrast to previous reports for a peptidyl carrier protein from a non-ribosomal peptide synthetase, no obvious structural differences between apo- and holo-DltC forms are observed. Solution NMR spectroscopy confirms these findings and demonstrates in addition that the two forms exhibit similar backbone dynamics on the ps-ns and ms timescales. High-resolution structures of the d-alanyl carrier protein (Dcp) DltC from Bacillus subtilis reveal equivalent conformations of apo- and holo-forms.,Zimmermann S, Pfennig S, Neumann P, Yonus H, Weininger U, Kovermann M, Balbach J, Stubbs MT FEBS Lett. 2015 Jul 17. pii: S0014-5793(15)00587-6. doi:, 10.1016/j.febslet.2015.07.008. PMID:26193422 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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