Crystal structure of the Campylobacter jejuni CmeC outer membrane channel. (6th May 2014)

• Record Type: Journal Article
• Authors: Su, Chih‐Chia; Radhakrishnan, Abhijith; Kumar, Nitin; Long, Feng; Bolla, Jani Reddy; Lei, Hsiang‐Ting; Delmar, Jared A.; Do, Sylvia V.; Chou, Tsung‐Han; Rajashankar, Kanagalaghatta R.; Zhang, Qijing; Yu, Edward W.
• Is Part Of: Protein science. Volume 23:Number 7(2014:Jul.)
• Page Start: 954
• Page End: 961
• Publication Date: 2014-05-06
• Subjects: Proteins -- Periodicals; 572.6
• DOI: 10.1002/pro.2478
• Languages: English
• ISSNs: 0961-8368

Abstract

<abstract abstract-type="main"> <title>Abstract</title> <p>As one of the world's most prevalent enteric pathogens, <italic>Campylobacter jejuni</italic> 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. <italic>Campylobacter</italic> 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 <italic>C. jejuni</italic>. This efflux complex spans the entire cell envelop of <italic>C. jejuni</italic> and mediates resistance to various antibiotics and toxic compounds. We here report the crystal structure of <italic>C. jejuni</italic> CmeC, the outer membrane component of the CmeABC tripartite multidrug efflux system. The structure reveals a possible mechanism for substrate export.</p> </abstract>