2f1m
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(New page: 200px<br /> <applet load="2f1m" size="450" color="white" frame="true" align="right" spinBox="true" caption="2f1m, resolution 2.71Å" /> '''Conformational flex...)
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Revision as of 07:01, 18 November 2007
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Conformational flexibility in the multidrug efflux system protein AcrA
Overview
Intrinsic resistance to multiple drugs in many gram-negative bacterial, pathogens is conferred by resistance nodulation cell division efflux, pumps, which are composed of three essential components as typified by the, extensively characterized Escherichia coli AcrA-AcrB-TolC system. The, inner membrane drug:proton antiporter AcrB and the outer membrane channel, TolC export chemically diverse compounds out of the bacterial cell, and, require the activity of the third component, the periplasmic protein AcrA., The crystal structures of AcrB and TolC have previously been determined, and we complete the molecular picture of the efflux system by presenting, the structure of a stable fragment of AcrA. The AcrA fragment resembles, the elongated sickle shape of its homolog Pseudomonas aeruginosa MexA, being composed of three domains: beta-barrel, lipoyl, and alpha-helical, hairpin. Notably, unsuspected conformational flexibility in the, alpha-helical hairpin domain of AcrA is observed, which has potential, mechanistic significance in coupling between AcrA conformations and TolC, channel opening.
About this Structure
2F1M is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Conformational flexibility in the multidrug efflux system protein AcrA., Mikolosko J, Bobyk K, Zgurskaya HI, Ghosh P, Structure. 2006 Mar;14(3):577-87. PMID:16531241
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