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- W2794687570 abstract "Significance LacY catalyzes stoichiometric symport of lactose and an H + across the membrane by an alternating access mechanism and is a paradigm for the major facilitator superfamily, the largest family of membrane transport proteins. The established mechanism is expanded here by kinetic studies involving binding and transport of greatly oversized substrates. Data demonstrate the high-affinity galactoside-specific interaction of LacY with large fluorescent substrates and, importantly, unrestricted accessibility of the sugar-binding site in the periplasmic-open conformation of the transporter. Moreover, oversized aglycones of galactosidic substrates do not preclude active transport; to accommodate a large-size ligand within occluded intermediate, it is likely that in the highly flexible LacY molecule additional movements in helical bends and kinks occur during the formation of extra space." @default.
- W2794687570 created "2018-04-06" @default.
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- W2794687570 date "2018-03-30" @default.
- W2794687570 modified "2023-09-23" @default.
- W2794687570 title "Oversized galactosides as a probe for conformational dynamics in LacY" @default.
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- W2794687570 doi "https://doi.org/10.1073/pnas.1800706115" @default.
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