Crystal structure of the Campylobacter jejuni CmeC outer membrane channelCrystal structure of the Campylobacter jejuni CmeC outer membrane channel

Structural highlights

4mt4 is a 3 chain structure with sequence from Campylobacter jejuni. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.373Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q8RTE3_CAMJU

Publication Abstract from PubMed

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.

Crystal structure of the Campylobacter jejuni CmeC outer membrane channel.,Su CC, Radhakrishnan A, Kumar N, Long F, Bolla JR, Lei HT, Delmar JA, Do SV, Chou TH, Rajashankar KR, Zhang Q, Yu EW Protein Sci. 2014 Jul;23(7):954-61. doi: 10.1002/pro.2478. Epub 2014 May 6. PMID:24753291[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Su CC, Radhakrishnan A, Kumar N, Long F, Bolla JR, Lei HT, Delmar JA, Do SV, Chou TH, Rajashankar KR, Zhang Q, Yu EW. Crystal structure of the Campylobacter jejuni CmeC outer membrane channel. Protein Sci. 2014 Jul;23(7):954-61. doi: 10.1002/pro.2478. Epub 2014 May 6. PMID:24753291 doi:http://dx.doi.org/10.1002/pro.2478

4mt4, resolution 2.37Å

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