PMID: 7032594Dec 21, 1981Paper

Lactose-H+(-OH) transport system of Escherichia coli. Multistate gated pore model based on half-sites stoichiometry for high-affinity substrate binding in a symmetrical dimer

Biochimica Et Biophysica Acta
F J Lombardi

Abstract

A model is proposed for the D-galactoside-H+(-OH) transporter of Escherichia coli that accounts for essentially all the experimental observations established for this system to date. In this model, the functional unit is postulated to be a dimer (consisting of two copies of lac Y-specified polypeptide) which spans the membrane with a 2-fold symmetry axis in the membrane plane (Lancaster, J.R. (1978) J. Theor. Biol. 75, 35-50). The functional dimer is assumed to possess a single pore flanked by an inner gate (gi) and an outer gate (go) and encompassing two oppositely oriented galactoside binding sites, designated m and mu. When go is open and gi is closed under non-energized conditions, binding site m adopts a configuration defined as State A (i.e., moA) exhibiting high affinity toward Class Ga galactosides (thiodigalactoside, melibiose, alpha-p-nitrophenygalactoside) but low affinity for Class Gb galactosides (lactose, beta-o-nitrophenylgalactoside, beta-isopropylthiogalactoside), whereas binding site mu adopts State B (i.e., muoB) displaying relatively high affinity toward Class Gb galactosides but comparatively low affinity for Class Ga galactosides; further, each moA : muoB dimer contains one thiol group whose reaction with ...Continue Reading

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Citations

Aug 1, 1990·Journal of Bioenergetics and Biomembranes·P J Henderson
Jan 1, 1983·The Journal of Membrane Biology·R J Turner
Dec 1, 1991·Bioscience Reports·P J Henderson
Jun 10, 2014·Cell Reports·David C MarcianoOlivier Lichtarge

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