Topology and function of the Na+/proline transporter of Escherichia coli, a member of the Na+/solute cotransporter family (Q47729694)

5 February 2018

review article

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title

Topology and function of the Na+/proline transporter of Escherichia coli, a member of the Na+/solute cotransporter family (English)

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5 February 2018

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H Jung

1

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5 February 2018

publication date

1 June 1998

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5 February 2018

Biochimica et Biophysica Acta

published in

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5 February 2018

volume

1365

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5 February 2018

issue

1-2

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5 February 2018

page(s)

60-64

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5 February 2018

A major superfamily of transmembrane facilitators that catalyse uniport, symport and antiport

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7 January 2021

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Aspartate 55 in the Na+/proline permease of Escherichia coli is essential for Na+-coupled proline uptake.

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Ser57 in the Na+/proline permease of Escherichia coli is critical for high-affinity proline uptake.

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Sugar binding to Na+/glucose cotransporters is determined by the carboxyl-terminal half of the protein.

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Sodium ion and proline binding sites in the Na+/proline symport carrier of Escherichia coli

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Orientation of the carboxyl terminus of the Na+/proline symport carrier in Escherichia coli

7 January 2021

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Determination of a transmembrane segment using cysteine-scanning mutants of transposon Tn10-encoded metal-tetracycline/H+ antiporter.

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Membrane topology of the human Na+/glucose cotransporter SGLT1

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Membrane topology of the melibiose permease of Escherichia coli studied by melB-phoA fusion analysis.

7 January 2021

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10.1016/S0005-2728(98)00044-9

7 January 2021

Identifiers

DOI

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5 February 2018

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5 February 2018