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.
- Registered users only
View at publisher
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.
1 download since deposited on 27 Jul 2009
0 downloads since 12 months
|Item Type:||Journal Article, refereed, original work|
|Communities & Collections:||04 Faculty of Medicine > Department of Biochemistry
07 Faculty of Science > Department of Biochemistry
|DDC:||570 Life sciences; biology|
|Deposited On:||27 Jul 2009 15:24|
|Last Modified:||27 Nov 2013 19:48|
Users (please log in): suggest update or correction for this item
Repository Staff Only: item control page