Structural highlights
Function
ACRB_ECOLI AcrAB is a drug efflux protein with a broad substrate specificity.[1] [2] [3]
Publication Abstract from PubMed
AcrB is an inner membrane resistance-nodulation-cell division efflux pump and is part of the AcrAB-TolC tripartite efflux system. We have determined the crystal structure of AcrB with bound Linezolid at a resolution of 3.5 A. The structure shows that Linezolid binds to the A385/F386 loops of the symmetric trimer of AcrB. A conformational change of a loop in the bottom of the periplasmic cleft is also observed.
Crystal structure of AcrB complexed with linezolid at 3.5 A resolution.,Hung LW, Kim HB, Murakami S, Gupta G, Kim CY, Terwilliger TC J Struct Funct Genomics. 2013 Jun;14(2):71-5. doi: 10.1007/s10969-013-9154-x., Epub 2013 May 15. PMID:23673416[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Murakami S, Nakashima R, Yamashita E, Matsumoto T, Yamaguchi A. Crystal structures of a multidrug transporter reveal a functionally rotating mechanism. Nature. 2006 Sep 14;443(7108):173-9. Epub 2006 Aug 16. PMID:16915237 doi:10.1038/nature05076
- ↑ Seeger MA, Schiefner A, Eicher T, Verrey F, Diederichs K, Pos KM. Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism. Science. 2006 Sep 1;313(5791):1295-8. PMID:16946072 doi:313/5791/1295
- ↑ Sennhauser G, Amstutz P, Briand C, Storchenegger O, Grutter MG. Drug export pathway of multidrug exporter AcrB revealed by DARPin inhibitors. PLoS Biol. 2007 Jan;5(1):e7. PMID:17194213 doi:10.1371/journal.pbio.0050007
- ↑ Hung LW, Kim HB, Murakami S, Gupta G, Kim CY, Terwilliger TC. Crystal structure of AcrB complexed with linezolid at 3.5 A resolution. J Struct Funct Genomics. 2013 Jun;14(2):71-5. doi: 10.1007/s10969-013-9154-x., Epub 2013 May 15. PMID:23673416 doi:10.1007/s10969-013-9154-x
