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Structure–function analysis of the ATP‐driven glycolipid efflux pump DevBCA reveals complex organization with TolC/HgdD
Author(s) -
Staron Peter,
Forchhammer Karl,
Maldener Iris
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.12.004
Subject(s) - periplasmic space , efflux , inner membrane , bacterial outer membrane , glycolipid , chemistry , microbiology and biotechnology , function (biology) , biochemistry , chemiosmosis , biophysics , membrane , biology , escherichia coli , atp synthase , enzyme , gene
In Gram‐negative bacteria, trans‐envelope efflux pumps have periplasmic membrane fusion proteins (MFPs) as essential components. MFPs act as mediators between outer membrane factors (OMFs) and inner membrane factors (IMFs). In this study, structure–function relations of the ATP‐driven glycolipid efflux pump DevBCA‐TolC/HgdD from the cyanobacterium Anabaena sp. PCC 7120 were analyzed. The binding of the MFP DevB to the OMF TolC absolutely required the respective tip‐regions. The interaction of DevB with the IMF DevAC mainly involved the β‐barrel and the lipoyl domain. Efficient binding to DevAC and TolC, substrate recognition and export activity by DevAC were dependent on stable DevB hexamers.