2003
DOI: 10.1074/jbc.m308253200
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Transmembrane Domain II of the Na+/Proline Transporter PutP of Escherichia coli Forms Part of a Conformationally Flexible, Cytoplasmic Exposed Aqueous Cavity within the Membrane

Abstract: The Na ؉ /proline transporter PutP of Escherichia coli is a member of a large family of Na ؉ /substrate symporters. Previous work on PutP suggests an involvement of the region ranging from Asp-55 to Gly-58 in binding of Na It is proposed that hydrophilic residues in the cytoplasmic half of TM II participate in the formation of an aqueous cavity in the membrane that allows Na ؉ and/or proline binding to residues located in the middle of the TM (e.g. Asp-55 and Ser-57). In addition, the data indicate that TM II … Show more

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Cited by 29 publications
(57 citation statements)
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“…2 A, G, and H). The equivalent position in PutP is also important (64,65). In NIS, the Na + at the Na2 site interacts with the -CO .…”
Section: Discussionmentioning
confidence: 99%
“…2 A, G, and H). The equivalent position in PutP is also important (64,65). In NIS, the Na + at the Na2 site interacts with the -CO .…”
Section: Discussionmentioning
confidence: 99%
“…Although speculative, such inferences may be appropriate since receptor B proteins show distant homology to these transporters, leading to their classification as a subgroup of the amino acid-polyamine-organocation superfamily (17). If the molecular basis of transport in prokaryotic amino acid transporters does represent a functional precedent for germinant-receptor B proteins, then it seems likely that residues that participate directly in germinant binding are also to be found in TM domains, since this is where ligand binding sites in a number of amino acid transporters are often located (24,25,36). The observation that residues spanning TM9 and TM10 in GerVB confer proline recognition to the GerUV fusion protein while OL5 residues alone do not would appear to substantiate this hypothesis.…”
Section: Discussionmentioning
confidence: 99%
“…Under a constant flow of watersaturated air, and while stirring magnetically, 10 mM potassium ascorbate and 100 M PMS (final concentration) were added, and the proton motive force was allowed to develop for 2 min. Then, [1,[5][6][7][8][9][10][11][12][13][14] C]citrate (114 mCi/mmol Amersham Biosciences) was added to a final concentration of 4.4 M. The uptake was stopped by the addition of 2 ml of ice-cold 0.1 M LiCl, followed by immediate filtration over cellulose nitrate filters (0.45 m, pore size). The filters were washed once with 2 ml of the 0.1 M LiCl solution and assayed for radioactivity.…”
Section: Methodsmentioning
confidence: 99%