PMID:15582398
| Citation |
Eswaran, J, Koronakis, E, Higgins, MK, Hughes, C and Koronakis, V (2004) Three's company: component structures bring a closer view of tripartite drug efflux pumps. Curr. Opin. Struct. Biol. 14:741-7 |
|---|---|
| Abstract |
Bacterial multidrug resistance is a serious clinical problem and is commonly conferred by tripartite efflux 'pumps' in the prokaryotic cell envelope. Crystal structures of the three components of a drug efflux pump have now been solved: the outer membrane TolC exit duct in the year 2000, the inner membrane AcrB antiporter in 2002 and the periplasmic adaptor MexA in 2004. These structures have enhanced our understanding of the principles underlying pump assembly and operation, and present pumps as new drug targets. |
| Links |
PubMed Online version:10.1016/j.sbi.2004.10.003 |
| Keywords |
Animals; Anti-Bacterial Agents/chemistry; Anti-Bacterial Agents/metabolism; Bacterial Outer Membrane Proteins/chemistry; Bacterial Outer Membrane Proteins/metabolism; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Biological Transport, Active/physiology; Carrier Proteins/chemistry; Carrier Proteins/metabolism; Cell Membrane/chemistry; Cell Membrane/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Humans; Membrane Proteins/chemistry; Membrane Proteins/metabolism; Membrane Transport Proteins/chemistry; Membrane Transport Proteins/metabolism; Models, Biological; Models, Chemical; Models, Molecular; Multidrug Resistance-Associated Proteins; Protein Conformation; Structure-Activity Relationship |
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