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Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-19886

Sennhauser, G; Bukowska, M A; Briand, C; Grütter, M G (2009). Crystal structure of the multidrug exporter MexB from Pseudomonas aeruginosa. Journal of Molecular Biology, 389(1):134-145.

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Abstract

We report here the crystal structure of the Pseudomonas aeruginosa multidrug exporter MexB, an intensively studied member of the resistance-nodulation-cell division family of secondary active transporters, at 3.0 A. MexB forms an asymmetric homotrimer where each subunit adopts a different conformation representing three snapshots of the transport cycle similar to the recently determined structures of its close homologue AcrB from Escherichia coli, so far the sole structurally characterized member of the superfamily. As for AcrB, the conformations of two subunits can be clearly assigned to either the binding step or the extrusion step in the transport process. Unexpectedly, a remarkable conformational shift in the third subunit is observed in MexB, which has potential implications for the assembly of the tripartite MexAB-OprM drug efflux system. Furthermore, an n-dodecyl-d-maltoside molecule was found bound to the internal multidrug-binding cavity, which might indicate that MexB binds and transports detergent molecules as substrates. As the only missing piece of the puzzle in the MexAB-OprM system, the X-ray structure of MexB completes the molecular picture of the major pump mediating intrinsic and acquired multidrug resistance in P. aeruginosa.

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > Institute of Biochemistry
07 Faculty of Science > Institute of Biochemistry
DDC:570 Life sciences; biology
Language:English
Date:2009
Deposited On:27 Jul 2009 17:24
Last Modified:27 Nov 2013 20:48
Publisher:Elsevier
ISSN:0022-2836
Publisher DOI:10.1016/j.jmb.2009.04.001
PubMed ID:19361527
Citations:Web of Science®. Times Cited: 58
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