Transient conformers of LacY are trapped by nanobodies

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Correction for Smirnova et al., Transient conformers of LacY are trapped by nanobodies.

The lactose permease of Escherichia coli (LacY), a highly dynamic membrane protein, catalyzes symport of a galactopyranoside and an H(+) by using an alternating access mechanism, and the transport cycle involves multiple conformational states. Single-domain camelid nanobodies (Nbs) developed against a LacY mutant immobilized in an outward (periplasmic)-open conformation bind to the flexible WT ...

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Outward-facing conformers of LacY stabilized by nanobodies.

The lactose permease of Escherichia coli (LacY), a highly dynamic polytopic membrane protein, catalyzes stoichiometric galactoside/H(+) symport by an alternating access mechanism and exhibits multiple conformations, the distribution of which is altered by sugar binding. We have developed single-domain camelid nanobodies (Nbs) against a LacY mutant in an outward (periplasmic)-open conformation t...

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Sugar recognition by CscB and LacY.

The sucrose permease (CscB) and lactose permease (LacY) of Escherichia coli belong to the oligosaccharide/H(+) symporter subfamily of the major facilitator superfamily, and both catalyze sugar/H(+) symport across the cytoplasmic membrane. Thus far, there is no common substrate for the two permeases; CscB transports sucrose, and LacY is highly specific for galactopyranosides. Determinants for Cs...

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ژورنال

عنوان ژورنال: Proceedings of the National Academy of Sciences

سال: 2015

ISSN: 0027-8424,1091-6490

DOI: 10.1073/pnas.1519485112