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J.S. Lolkema, and D.J. Slotboom Classification of 29 families of secondary transport proteins into a single structural class using hydropathy profile analysis J Mol Biol 327 2003 901 909
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Structure and mechanism of the lactose permease of Escherichia coli
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••], these studies determined the first two structures of members of the major facilitator superfamily transporters, which are the most abundant family of transporters in nature. The structures confirm and extend the massive amount of experimental data that is available for this type of transporter. These transporter proteins consist of two homologous domains, each comprising six transmembrane segments connected by a large loop.
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Mechanism of ammonia transport by Amt/MEP/Rh: structure of AmtB at 1.35 Å
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0037122805
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X-ray structure of a ClC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity
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0030739372
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M. Bandell, V. Ansanay, N. Rachidi, S. Dequin, and J.S. Lolkema Membrane potential generating malate (MleP) and citrate (CitP) transporters of lactic acid bacteria are homologous proteins. Substrate specificity of the 2-hydroxy-carboxylate transporter family J Biol Chem 272 1997 18140 18146
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0034213082
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0042026505
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Accessibility of cysteine residues in a cytoplasmic loop of CitS of Klebsiella pneumoniae is controlled by the catalytic state of the transporter
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I. Sobczak, and J.S. Lolkema Accessibility of cysteine residues in a cytoplasmic loop of CitS of Klebsiella pneumoniae is controlled by the catalytic state of the transporter Biochemistry 42 2003 9789 9796
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Biochemistry
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Sobczak, I.1
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0037457976
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Conserved residues R420 and Q428 in a cytoplasmic loop of the citrate/malate transporter CimH of Bacillus subtilis are accessible from the external face of the membrane
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B.P. Krom, and J.S. Lolkema Conserved residues R420 and Q428 in a cytoplasmic loop of the citrate/malate transporter CimH of Bacillus subtilis are accessible from the external face of the membrane Biochemistry 42 2003 467 474 Studies of the accessibility of two cysteine residues engineered at sites in a cytoplasmic loop of a member of the 2-hydroxycarboxylate transporter family provides the first evidence for a pore-loop structure in the proteins.
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