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  • Title: 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.
    Author: Lombardi FJ.
    Journal: Biochim Biophys Acta; 1981 Dec 21; 649(3):661-79. PubMed ID: 7032594.
    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 N-ethylmaleimide inactivates the transporter unless blocked by galactoside binding at site moA, while the second homologous thiol of the dimer is unreactive toward thiol reagents. Translocation of the moA : muoB dimer involves closing of go followed by opening of gi, and causes the two thiols (as well as sites m and mu) to interchange roles in a symmetrical fashion: moA : muoB in equilibrium miB : muiA. In the presence of a substantial (negative) transmembrane delta potential of muH+, the m : mu dimer is postulated to undergo an electrogenic protein conformation change to a second form, *(m : mu), in which both sites m and mu possess low affinity toward internal Class Gb substrates; galactoside transport in both m : mu and *(m : mu) is assumed to be coupled to H+-symport (-OH-antiport) with a stoichiometry of approximately 1 : 1. Finally, five characteristic predictions of the half-sites model are outlined for further tests of its validity.
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