Purification, crystallization and preliminary diffraction studies of AcrB, an inner‐membrane multi‐drug efflux protein | Zendy

Pos Klaas M. | Zendy; Diederichs Kay | Zendy

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Purification, crystallization and preliminary diffraction studies of AcrB, an inner‐membrane multi‐drug efflux protein

Author(s) -

Pos Klaas M.,

Diederichs Kay

Publication year - 2002

Publication title -

acta crystallographica section d

Language(s) - English

Resource type - Journals

ISSN - 1399-0047

DOI - 10.1107/s0907444902013963

Subject(s) - efflux , escherichia coli , multidrug resistance associated proteins , novobiocin , inner membrane , transporter , crystallization , bacterial outer membrane , membrane protein , bacteria , multiple drug resistance , antibiotics , biology , transport protein , microbiology and biotechnology , biochemistry , chemistry , membrane , atp binding cassette transporter , genetics , gene , organic chemistry

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 R 32, with unit‐cell parameters a = b = 143, c = 513 Å; the crystals diffract to 3.0 Å resolution.

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