Assignment of the outer-membrane-subunit-selective domain of the membrane fusion protein in the tripartite xenobiotic efflux pump ofPseudomonas aeruginosa
Author:
Publisher
Oxford University Press (OUP)
Subject
Genetics,Molecular Biology,Microbiology
Link
http://academic.oup.com/femsle/article-pdf/254/1/101/19118850/254-1-101.pdf
Reference41 articles.
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2. Akama H , Kanemaki M , Yoshimura M , Tsukihara T , Kashiwagi T , Yoneyama H , Narita S , Nakagawa A & Nakae T (2004a) Crystal structure of the drug discharge outer membrane protein, OprM, of Pseudomonas aeruginosa: dual modes of membrane anchoring and occluded cavity end. J Biol Chem 279: 52816 â 52819.
3. Akama H , Matsuura T , Kashiwagi S , Yoneyama H , Narita S , Tsukihara T , Nakagawa A & Nakae T (2004b) Crystal structure of the membrane fusion protein, MexA, of the multidrug transporter in Pseudomonas aeruginosa. J Biol Chem 279: 25939 â 25942.
4. Chuanchuen R , Murata T , Gotoh N & Schweizer HP (2005) Substrate-dependent utilization of OprM or OpmH by the Pseudomonas aeruginosa MexJK efflux pump. Antimicrob Agents Chemother 49: 2133 â 2136.
5. Dinh T , Paulsen IT & Saier MH Jr (1994) A family of extracytoplasmic proteins that allow transport of large molecules across the outer membranes of gram-negative bacteria. J Bacteriol 176: 3825 â 3831.
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