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• W2003586215 abstract "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." @default.
• W2003586215 created "2016-06-24" @default.
• W2003586215 creator A5015013845 @default.
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• W2003586215 creator A5048175299 @default.
• W2003586215 date "2013-12-17" @default.
• W2003586215 modified "2023-09-27" @default.
• W2003586215 title "Structure-function analysis of the ATP-driven glycolipid efflux pump DevBCA reveals complex organization with TolC/HgdD" @default.
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• W2003586215 doi "https://doi.org/10.1016/j.febslet.2013.12.004" @default.
• W2003586215 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24361095" @default.
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