2n5w | pdb_00002n5w

The NMR solution structure of octyl-tridecaptin A1 in DPC micelles

spinqualitylabelsall models 2n5w, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2n5w is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: 28J, 4FO, 4N3, DAB Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Tridecaptin A1 (TriA1) is a nonribosomal lipopeptide with selective antimicrobial activity against Gram-negative bacteria. Here we show that TriA1 exerts its bactericidal effect by binding to the bacterial cell-wall precursor lipid II on the inner membrane, disrupting the proton motive force. Biochemical and biophysical assays show that binding to the Gram-negative variant of lipid II is required for membrane disruption and that only the proton gradient is dispersed. The NMR solution structure of TriA1 in dodecylphosphocholine micelles with lipid II has been determined, and molecular modeling was used to provide a structural model of the TriA1-lipid II complex. These results suggest that TriA1 kills Gram-negative bacteria by a mechanism of action using a lipid-II-binding motif. Antimicrobial lipopeptide tridecaptin A1 selectively binds to Gram-negative lipid II.,Cochrane SA, Findlay B, Bakhtiary A, Acedo JZ, Rodriguez-Lopez EM, Mercier P, Vederas JC Proc Natl Acad Sci U S A. 2016 Oct 11;113(41):11561-11566. Epub 2016 Sep 29. PMID:27688760 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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