2N5W

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

2N5W の概要

• エントリーDOI: 10.2210/pdb2n5w/pdb
• NMR情報: BMRB: 25737
• 分子名称: Octyl-tridecaptin A1 (1 entity in total)
• 機能のキーワード: tridecaptin a1, lipopeptide, antimicrobial, antibiotic, non-ribosomal, antimicrobial protein
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1520.77

構造登録者

Cochrane, S.A.,Findlay, B.,Bakhtiary, A.,Acedo, J.Z.,Rodriguez-Lopez, E.M.,Vederas, J.C. (登録日: 2015-08-01, 公開日: 2016-09-28, 最終更新日: 2023-11-15)

主引用文献

Cochrane, S.A.,Findlay, B.,Bakhtiary, A.,Acedo, J.Z.,Rodriguez-Lopez, E.M.,Mercier, P.,Vederas, J.C.
Antimicrobial lipopeptide tridecaptin A1 selectively binds to Gram-negative lipid II.
Proc.Natl.Acad.Sci.USA, 113:11561-11566, 2016

PubMed Abstract: Tridecaptin A (TriA) is a nonribosomal lipopeptide with selective antimicrobial activity against Gram-negative bacteria. Here we show that TriA 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 TriA in dodecylphosphocholine micelles with lipid II has been determined, and molecular modeling was used to provide a structural model of the TriA-lipid II complex. These results suggest that TriA kills Gram-negative bacteria by a mechanism of action using a lipid-II-binding motif.

PubMed: 27688760
DOI: 10.1073/pnas.1608623113

実験手法

SOLUTION NMR