Literature DB >> 24753291

Crystal structure of the Campylobacter jejuni CmeC outer membrane channel.

Chih-Chia Su1, Abhijith Radhakrishnan, Nitin Kumar, Feng Long, Jani Reddy Bolla, Hsiang-Ting Lei, Jared A Delmar, Sylvia V Do, Tsung-Han Chou, Kanagalaghatta R Rajashankar, Qijing Zhang, Edward W Yu.   

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.
© 2014 The Protein Society.

Entities:  

Keywords:  Campylobacter jejuni; efflux channel; membrane protein; multidrug resistance; resistance-nodulation-cell division

Mesh:

Substances:

Year:  2014        PMID: 24753291      PMCID: PMC4088979          DOI: 10.1002/pro.2478

Source DB:  PubMed          Journal:  Protein Sci        ISSN: 0961-8368            Impact factor:   6.725


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