6E00

Structure of a N-Me-p-iodo-D-Phe1,N-Me-D-Gln4,Lys10-teixobactin analogue

6E00 の概要

• エントリーDOI: 10.2210/pdb6e00/pdb
• 関連するBIRD辞書のPRD_ID: PRD_002317
• 分子名称: N-Me-p-iodo-D-Phe1,N-Me-D-Gln4,Lys10-teixobactin analogue, SULFATE ION (3 entities in total)
• 機能のキーワード: antibiotic, teixobactin, fibril, helix
• 由来する生物種: Eleftheria terrae
• タンパク質・核酸の鎖数: 32
• 化学式量合計: 47087.33

構造登録者

Nowick, J.S.,Yang, H.,Wierzbicki, M. (登録日: 2018-07-05, 公開日: 2018-10-17, 最終更新日: 2023-11-15)

主引用文献

Yang, H.,Wierzbicki, M.,Du Bois, D.R.,Nowick, J.S.
X-ray Crystallographic Structure of a Teixobactin Derivative Reveals Amyloid-like Assembly.
J. Am. Chem. Soc., 140:14028-14032, 2018

PubMed Abstract: This paper describes the X-ray crystallographic structure of a derivative of the antibiotic teixobactin and shows that its supramolecular assembly through the formation of antiparallel β-sheets creates binding sites for oxyanions. An active derivative of teixobactin containing lysine in place of allo-enduracididine assembles to form amyloid-like fibrils, which are observed through a thioflavin T fluorescence assay and by transmission electron microscopy. A homologue, bearing an N-methyl substituent, to attenuate fibril formation, and an iodine atom, to facilitate X-ray crystallographic phase determination, crystallizes as double helices of β-sheets that bind sulfate anions. β-Sheet dimers are key subunits of these assemblies, with the N-terminal methylammonium group of one monomer and the C-terminal macrocycle of the other monomer binding each anion. These observations suggest a working model for the mechanism of action of teixobactin, in which the antibiotic assembles and the assemblies bind lipid II and related bacterial cell wall precursors on the surface of Gram-positive bacteria.

PubMed: 30296063
DOI: 10.1021/jacs.8b07709

実験手法

X-RAY DIFFRACTION (2.2 Å)