Evidence map›Paper›PMID 23950222›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Structure of the YajR transporter suggests a transport mechanism based on the conserved motif A.

Daohua Jiang, Yan Zhao, Xianping Wang, Junping Fan, Jie Heng, Xuehui Liu, Wei Feng, Xusheng Kang, Bo Huang, Jianfeng Liu and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 115 papers.

0numbers the graph read from it
0cells of the map it votes in
115citing papers in PubMed
10.0field-weighted citation impact, top 2% of its field
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

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

115 citing papers in PubMed, 198 citations in OpenAlex.

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  8. Energetic and structural control of polyspecificity in a multidrug transporter.Proceedings of the National Academy of Sciences of the United States of America · 2025
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55 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 at 3 institutions in 1 country.

Daohua JiangNational Laboratory of Macromolecules, National Center of Protein Science, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
Yan Zhao
Xianping Wang
Junping Fan
Jie Heng
Xuehui Liu
Wei Feng
Xusheng Kang
Bo Huang
Jianfeng Liu
Xuejun Cai Zhang
Chinese Academy of Sciences · CNInstitute of Biophysics · CNHuazhong University of Science and Technology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The major facilitator superfamily (MFS) is the largest family of secondary active transporters and is present in all life kingdoms. Detailed structural basis of the substrate transport and energy-coupling mechanisms of these proteins remain to be elucidated. YajR is a putative proton-driven MFS transporter found in many Gram-negative bacteria. Here we report the crystal structure of Escherichia coli YajR at 3.15 Å resolution in an outward-facing conformation. In addition to having the 12 canonical transmembrane helices, the YajR structure includes a unique 65-residue C-terminal domain which is independently stable. The structure is unique in illustrating the functional role of "sequence motif A." This highly conserved element is seen to stabilize the outward conformation of YajR and suggests a general mechanism for the conformational change between the inward and outward states of the MFS transporters.

Indexed as

Amino Acid MotifsProtein Structure, TertiaryAmino Acid SequenceBinding SitesBiological TransportCrystallography, X-RayElectrophoresis, Polyacrylamide GelEscherichia coliEscherichia coli ProteinsMembrane Transport ProteinsModels, MolecularMolecular Sequence DataMutationProtein ConformationProtein Structure, SecondarySequence Homology, Amino AcidEscherichia coli ProteinsMembrane Transport ProteinsYajR protein, E colicharge-dipole interactioncharge relaymembrane potentialprotonation

Identifiers

PMID23950222
PMCPMC3767500
OpenAlexW2112537322

What OpenQuestion holds

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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.