Evidence map›Paper›PMID 21131908›Full record

ArticleThe EMBO journal2011

Crystal structure of a prokaryotic homologue of the mammalian oligopeptide-proton symporters, PepT1 and PepT2.

Simon Newstead, David Drew, Alexander D Cameron, Vincent L G Postis, Xiaobing Xia, Philip W Fowler, Jean C Ingram, Elisabeth P Carpenter, Mark S P Sansom, Michael J McPherson and 2 more

Abstract read
In one paragraph

Article in The EMBO journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 138 papers.

0numbers the graph read from it
0cells of the map it votes in
138citing papers in PubMed
12.6field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

138 citing papers in PubMed, 307 citations in OpenAlex.

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78 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors at 6 institutions in 2 countries.

Simon NewsteadDivision of Molecular Biosciences, Membrane Protein Crystallography Group, Imperial College London, London, UK. simon.newstead@bioch.ox.ac.uk
David Drew
Alexander D Cameron
Vincent L G Postis
Xiaobing Xia
Philip W Fowler
Jean C Ingram
Elisabeth P Carpenter
Mark S P Sansom
Michael J McPherson
Stephen A Baldwin
So Iwata
University of Leeds · GBDiamond Light Source · GBJapan Science and Technology Agency · JPUniversity of Oxford · GBImperial College London · GBInstitute of Structural and Molecular Biology · GB

Funding

Biotechnology and Biological Sciences Research Council BB/G023425/1Biotechnology and Biological Sciences Research Council BBS/B/14418Wellcome TrustWellcome Trust 062164/Z/00/Z
6 · The paper itself

Abstract

PepT1 and PepT2 are major facilitator superfamily (MFS) transporters that utilize a proton gradient to drive the uptake of di- and tri-peptides in the small intestine and kidney, respectively. They are the major routes by which we absorb dietary nitrogen and many orally administered drugs. Here, we present the crystal structure of PepT(So), a functionally similar prokaryotic homologue of the mammalian peptide transporters from Shewanella oneidensis. This structure, refined using data up to 3.6 Å resolution, reveals a ligand-bound occluded state for the MFS and provides new insights into a general transport mechanism. We have located the peptide-binding site in a central hydrophilic cavity, which occludes a bound ligand from both sides of the membrane. Residues thought to be involved in proton coupling have also been identified near the extracellular gate of the cavity. Based on these findings and associated kinetic data, we propose that PepT(So) represents a sound model system for understanding mammalian peptide transport as catalysed by PepT1 and PepT2.

Indexed as

Models, MolecularBinding SitesCrystallographyPeptide Transporter 1ShewanellaSymportershydrogen-coupled oligopeptide transporter PepT2Peptide Transporter 1Symporters

Identifiers

PMID21131908
PMCPMC3025455
OpenAlexW2139565537

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.