4MT4

Crystal structure of the Campylobacter jejuni CmeC outer membrane channel

4MT4 の概要

• エントリーDOI: 10.2210/pdb4mt4/pdb
• 分子名称: CmeC, (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: beta barrel, transport protein
• 由来する生物種: Campylobacter jejuni
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 169419.99

構造登録者

Su, C.-C.,Yu, E.W. (登録日: 2013-09-19, 公開日: 2014-09-24, 最終更新日: 2024-10-16)

主引用文献

Su, C.C.,Radhakrishnan, A.,Kumar, N.,Long, F.,Bolla, J.R.,Lei, H.T.,Delmar, J.A.,Do, S.V.,Chou, T.H.,Rajashankar, K.R.,Zhang, Q.,Yu, E.W.
Crystal structure of the Campylobacter jejuni CmeC outer membrane channel.
Protein Sci., 23:954-961, 2014

PubMed Abstract: As one of the world's most prevalent enteric pathogens, Campylobacter jejuni is a major causative agent of human enterocolitis and is responsible for more than 400 million cases of diarrhea each year. The impact of this pathogen on children is of particular significance. Campylobacter has developed resistance to many antimicrobial agents via multidrug efflux machinery. The CmeABC tripartite multidrug efflux pump, belonging to the resistance-nodulation-cell division (RND) superfamily, plays a major role in drug resistant phenotypes of C. jejuni. This efflux complex spans the entire cell envelop of C. jejuni and mediates resistance to various antibiotics and toxic compounds. We here report the crystal structure of C. jejuni CmeC, the outer membrane component of the CmeABC tripartite multidrug efflux system. The structure reveals a possible mechanism for substrate export.

PubMed: 24753291
DOI: 10.1002/pro.2478

実験手法

X-RAY DIFFRACTION (2.373 Å)