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- concentration wave of E. coli bacteria in a microchannel
- Amphiphilic Poly(ethylene oxide)-block-poly(butadiene-graft-liquid crystal) Copolymers: Synthesis and Self-Assembly in Water
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- schematic model of the coupling between the non equivalent catalytic sites of ABC transporters
- schematic model of the coupling between the non equivalent catalytic sites of ABC transporters
- schematic model of the coupling between the equivalent catalytic sites of ABC transporters
- Tubular to planar membranes upon conformational changes of BmrA, a ABC transporter
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Tubular to planar membranes upon conformational changes of BmrA, a ABC transporter

BmrA, a bacterial homodimeric ABC transporter has been reconstituted in a lipid bilayer at high protein density. BmrA provides a ATP dependant efflux transport of drugs including antibiotics and anticancer agents. BmrA trapped in different catalytic states has been reconstituted in lipid membrane and the result analyzed by electron microscopy. (A) BmrA wild type in absence of ATP. Formation of tubular membranes (B) WT in presence of ATP. Formation of planar membrane. (C) E504Q mutant able to bind but not to hydrolyze ATP. Recosntitution in absence of ATP leads to the formation of tubular membranes. (D) Reconstitution in presence of ATP leads to the formation of planar membrane. Overall, the data are show that binding rather than hydrolysis of ATP is the drivent force of a large conformational change of BmrA, likely related to the drug translocation. From
Orelle, C., Gubellini, F., Durand, A., Marco, S., Lévy, D., Gros, P., Di Pietro, A., and Jault, J. M. (2008) Conformational change induced by ATP binding in the multidrug ATP-binding cassette transporter BmrA, Biochemistry 47, 2404-2412.

