6BR4

Crystal structure of Escherichia coli DsbA in complex with {N}-methyl-1-(3-thiophen-2-ylphenyl)methanamine

6BR4 の概要

• エントリーDOI: 10.2210/pdb6br4/pdb
• 関連するPDBエントリー: 4wf5
• 分子名称: Thiol:disulfide interchange protein DsbA, ~{N}-methyl-1-(3-thiophen-2-ylphenyl)methanamine, COPPER (II) ION, ... (4 entities in total)
• 機能のキーワード: disulphide catalysts, thiol oxidase, virulence factor foldase, oxidoreductase
• 由来する生物種: Escherichia coli (strain K12)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 42640.44

構造登録者

Heras, B.,Totsika, M.,Paxman, J.J.,Wang, G.,Scanlon, M.J.,Martin, J.L. (登録日: 2017-11-29, 公開日: 2017-12-27, 最終更新日: 2024-11-20)

主引用文献

Totsika, M.,Vagenas, D.,Paxman, J.J.,Wang, G.,Dhouib, R.,Sharma, P.,Martin, J.L.,Scanlon, M.J.,Heras, B.
Inhibition of Diverse DsbA Enzymes in Multi-DsbA Encoding Pathogens.
Antioxid. Redox Signal., 29:653-666, 2018

PubMed Abstract: DsbA catalyzes disulfide bond formation in secreted and outer membrane proteins in bacteria. In pathogens, DsbA is a major facilitator of virulence constituting a target for antivirulence antimicrobial development. However, many pathogens encode multiple and diverse DsbA enzymes for virulence factor folding during infection. The aim of this study was to determine whether our recently identified inhibitors of Escherichia coli K-12 DsbA can inhibit the diverse DsbA enzymes found in two important human pathogens and attenuate their virulence.

PubMed: 29237285
DOI: 10.1089/ars.2017.7104

実験手法

X-RAY DIFFRACTION (1.99 Å)