5azs
From Proteopedia
Crystal structure of a membrane protein from Pseudomonas aeruginosa
Structural highlights
FunctionOPRJ_PSEAE Channel-forming component of a multidrug resistance efflux pump. Publication Abstract from PubMedThe genome of Pseudomonas aeruginosa encodes tripartite efflux pumps that extrude functionally and structurally dissimilar antibiotics from the bacterial cell. MexAB-OprM, MexCD-OprJ, MexEF-OprN, and MexXY-OprM are the main tripartite efflux pumps responsible for multidrug resistance in P. aeruginosa. The outer membrane factors OprN, OprJ, and OprM are essential components of functional tripartite efflux pumps. To elucidate the structural basis of multidrug resistance, we determined the crystal structures of OprN and OprJ. These structures revealed several features, including tri-acylation of the N-terminal cysteine, a small pore in the beta-barrel domain, and a tightly sealed gate in the alpha-barrel domain. Despite the overall similarity of OprN, OprJ, and OprM, a comparison of their structures and electrostatic distributions revealed subtle differences at the periplasmic end of the alpha-barrel domain. These results suggested that the overall structures of these outer membrane factors are specifically optimized for particular tripartite efflux pumps. Proteins 2016; 84:759-769. (c) 2016 Wiley Periodicals, Inc. Crystal structures of OprN and OprJ, outer membrane factors of multidrug tripartite efflux pumps of Pseudomonas aeruginosa.,Yonehara R, Yamashita E, Nakagawa A Proteins. 2016 Jun;84(6):759-69. doi: 10.1002/prot.25022. Epub 2016 Mar 9. PMID:26914226[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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