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• W2007257060 abstract "The LolCDE complex is an ATP-binding cassette transporter that mediates the release of newly synthesized lipoproteins from the cytoplasmic membrane of gram-negative bacteria, which results in the initiation of outer-membrane sorting of lipoproteins through the Lol pathway. LolCDE is composed of one copy each of membrane subunits LolC and LolE, and two copies of nucleotide-binding subunit LolD. In this study, we examined the membrane topology of LolC and LolE by PhoA fusion analysis. Both LolC and LolE were found to have four transmembrane segments with a large periplasmic loop exposed to the periplasm. Despite similarities in sequence and topology, the accessibility of a sulfhydryl reagent to Cys introduced into the periplasmic loop suggested that the structure of the periplasmic region differs between LolC and LolE. Inhibition of the release of lipoproteins by the sulfhydryl reagent supported a previous proposal that LolC and LolE have distinct functions." @default.
• W2007257060 created "2016-06-24" @default.
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• W2007257060 date "2009-10-23" @default.
• W2007257060 modified "2023-10-01" @default.
• W2007257060 title "Membrane Topology and Functional Importance of the Periplasmic Region of ABC Transporter LolCDE" @default.
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• W2007257060 doi "https://doi.org/10.1271/bbb.90451" @default.
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