PMID:12654283
| Citation |
Elkins, CA and Nikaido, H (2003) 3D structure of AcrB: the archetypal multidrug efflux transporter of Escherichia coli likely captures substrates from periplasm. Drug Resist. Updat. 6:9-13 |
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| Abstract |
Recent advances in structural biology have extended our understanding of the multiple drug efflux complex, AcrAB-TolC, of Escherichia coli. This tripartite complex and its homologs are the major mechanisms that give most Gram-negative bacteria their characteristic intrinsic resistance to a variety of lipophilic drugs, dyes, and detergents. Most recently, the structure of the transporter AcrB was elucidated at high resolution [Nature 419(2002)587]. It is a particularly significant achievement since integral membrane proteins are notoriously elusive structures for crystallography. The striking features of this trimeric pump, such as the presence of potential substrate-binding sites in the periplasmic domain and the possibility of direct interaction with the end of TolC tunnel, refine our understanding of the mode of action of this tripartite efflux transport complex. |
| Links | |
| Keywords |
Bacterial Outer Membrane Proteins/chemistry; Carrier Proteins/chemistry; Carrier Proteins/physiology; Crystallography, X-Ray; Drug Resistance, Multiple, Bacterial; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/physiology; Membrane Proteins/chemistry; Membrane Proteins/physiology; Membrane Transport Proteins; Models, Molecular; Multidrug Resistance-Associated Proteins; Periplasm/physiology; Protein Structure, Quaternary |
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