Evidence map›Paper›PMID 21423164›Full record

ArticleNature2011

Structure and mechanism of the uracil transporter UraA.

Feiran Lu, Shuo Li, Yang Jiang, Jing Jiang, He Fan, Guifeng Lu, Dong Deng, Shangyu Dang, Xu Zhang, Jiawei Wang and 1 more

Abstract read
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Article in Nature, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 100 papers.

0numbers the graph read from it
0cells of the map it votes in
100citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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

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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

100 citing papers in PubMed.

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  18. SLC26 Anion Transporters.Handbook of experimental pharmacology · 2024
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40 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

11 authors.

Feiran LuState Key Laboratory of Bio-membrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Shuo Li
Yang Jiang
Jing Jiang
He Fan
Guifeng Lu
Dong Deng
Shangyu Dang
Xu Zhang
Jiawei Wang
Nieng Yan

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The nucleobase/ascorbate transporter (NAT) proteins, also known as nucleobase/cation symporter 2 (NCS2) proteins, are responsible for the uptake of nucleobases in all kingdoms of life and for the transport of vitamin C in mammals. Despite functional characterization of the NAT family members in bacteria, fungi and mammals, detailed structural information remains unavailable. Here we report the crystal structure of a representative NAT protein, the Escherichia coli uracil/H(+) symporter UraA, in complex with uracil at a resolution of 2.8 Å. UraA has a novel structural fold, with 14 transmembrane segments (TMs) divided into two inverted repeats. A pair of antiparallel β-strands is located between TM3 and TM10 and has an important role in structural organization and substrate recognition. The structure is spatially arranged into a core domain and a gate domain. Uracil, located at the interface between the two domains, is coordinated mainly by residues from the core domain. Structural analysis suggests that alternating access of the substrate may be achieved through conformational changes of the gate domain.

Indexed as

Biological TransportCrystallography, X-RayEscherichia coliEscherichia coli ProteinsHydrogen BondingMembrane Transport ProteinsModels, BiologicalModels, MolecularProtein FoldingProtein Structure, SecondaryProtein Structure, TertiaryProtonsStructure-Activity RelationshipUracilEscherichia coli ProteinsMembrane Transport ProteinsProtonsUraA protein, E coliUracil

Identifiers

PMID21423164

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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.