Purification, crystallization and preliminary diffraction studies of AcrB, an inner-membrane multi-drug efflux protein.
Resistance of pathogens to antibiotics is often dependent on multi-drug export proteins that reside in the inner membrane of bacteria. This work describes the expression, purification, crystallization and preliminary crystallographic analysis of AcrB of Escherichia coli. Together with AcrA and TolC, AcrB forms a proton motive force dependent efflux pump of the resistance-nodulation-cell division (RND) transporter superfamily and is responsible for resistance towards many common antibiotics such as ciprofloxacin and novobiocin. AcrB crystallizes in space group R32, with unit-cell parameters a = b = 143, c = 513 A; the crystals diffract to 3.0 A resolution.
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D002352:Carrier Proteins; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000737:chemistry; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000302:isolation & purification; D008565:Membrane Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D027425:ATP-Binding Cassette, Sub-Family C Proteins; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification
D001426:Bacterial Proteins; D002352:Carrier Proteins; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D027425:ATP-Binding Cassette, Sub-Family C Proteins; D011994:Recombinant Proteins; C083496:AcrB protein, E coli