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The structure of the efflux pump AcrB in complex with bile acid

DOI: 10.1080/09687680802552257 DOI Help
PMID: 19023693 PMID Help

Authors: Mirjam M. Klepsch (Membrane Protein Laboratory, Imperial College, London) , Simon Newstead (Membrane Protein Laboratory, Imperial College, London) , Ralf Flaig (Diamond Light Source) , Jan-willem De Gier (Membrane Protein Laboratory, Imperial College, London) , Konstantinos Beis (Membrane Protein Laboratory, Imperial College, London) , David Drew (Membrane Protein Laboratory, Imperial College, London) , So Iwata (Diamond Light Source)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Molecular Membrane Biology , VOL 25 (8) , PAGES 677 - 682

State: Published (Approved)
Published: December 2008

Abstract: Gastrointestinal bacteria, like Escherichia coli, must remove bile acid to survive in the gut. Bile acid removal in E. coli is thought to be mediated primarily by the multidrug efflux pump, AcrB. Here, we present the structure of E. coli AcrB in complex with deoxycholate at 3.85 Å resolution. All evidence suggests that bile acid is transported out of the cell via the periplasmic vestibule of the AcrAB-TolC complex.

Keywords: X-Ray; Deoxycholic; Escherichia; Multidrug; Mutant Proteins

Subject Areas: Biology and Bio-materials


Beamlines: I04-Macromolecular Crystallography

Other Synchrotrons: ESRF