4MT4

Crystal structure of the Campylobacter jejuni CmeC outer membrane channel

Summary for 4MT4

• Entry DOI: 10.2210/pdb4mt4/pdb
• Descriptor: CmeC, (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE, SULFATE ION, ... (5 entities in total)
• Functional Keywords: beta barrel, transport protein
• Biological source: Campylobacter jejuni
• Total number of polymer chains: 3
• Total formula weight: 169419.99

Authors

Su, C.-C.,Yu, E.W. (deposition date: 2013-09-19, release date: 2014-09-24, Last modification date: 2024-10-16)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.373 Å)