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FEBS Lett. 2010 Apr 16;584(8):1493-7. doi: 10.1016/j.febslet.2010.02.066. Epub 2010 Mar 3.

Evidence that the C-terminus of OprM is involved in the assembly of the VceAB-OprM efflux pump.

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Department of Microbiology and Immunology, Texas Tech University Health Science Center, Lubbock, TX 79430, USA.


Although the architecture of tripartite multiple drug resistance (MDR) efflux pumps of Gram-negative bacteria has been well characterized, the means by which the components recognize each other and assemble into a functional pump remains obscure. In this study we present evidence that the C-terminal domain of the Pseudomonas aeruginosa OprM and the alpha-helical hairpin domain of Vibrio cholerae VceA play an important role in the recognition/specificity/recruitment step in the assembly of a functional, VceAB-OprM chimeric efflux pump. To our knowledge, this is the first evidence directly linking the C-terminal domain of an outer membrane efflux protein to its recruitment during the assembly of a tripartite efflux pump.

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