FEBS Letters
Volume 580, Issue 4 , Pages 1042-1048, 13 February 2006

The structures of MsbA: Insight into ABC transporter-mediated multidrug efflux

Edited by Gerrit van Meer

Department of Molecular Biology, The Scripps Research Institute, 10550 N. Torrey Pines Rd, CB105, La Jolla CA 92137, United States

Received 11 October 2005; received in revised form 7 November 2005; accepted 14 November 2005. published online 30 November 2005.

Abstract 

ATP-binding cassette (ABC) transporters are integral membrane proteins that couple ATP hydrolysis to the transport of various molecules across cellular membranes. Found in both prokaryotes and eukaryotes, a sub-group of these transporters are involved in the efflux of hydrophobic drugs and lipids, causing anti-microbial and chemotherapeutic multidrug resistance. In this review, we examine recent structural and functional analysis of the ABC transporter MsbA and implications on the mechanism of multidrug efflux.

Abbreviations: ABC, ATP binding cassette, ICD, intercellular domain, LPS, lipopolysaccharide, MDR, multidrug resistance, NBD, nucleotide binding domain, P-gp, P-glycoprotein, TMD, transmembrane binding domain, EM, electron microscopy

Keywords: Multidrug resistance, ABC transporter, Membrane protein, X-ray crystallography, MsbA, P-glycoprotein, LmrA

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PII: S0014-5793(05)01396-7

doi:10.1016/j.febslet.2005.11.033

FEBS Letters
Volume 580, Issue 4 , Pages 1042-1048, 13 February 2006