Evidence map›Paper›PMID 23341604›Full record

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

Inward-facing conformation of the zinc transporter YiiP revealed by cryoelectron microscopy.

Nicolas Coudray, Salvatore Valvo, Minghui Hu, Ralph Lasala, Changki Kim, Martin Vink, Ming Zhou, Davide Provasi, Marta Filizola, Juoehi Tao and 4 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 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
7.6field-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

61 citing papers in PubMed, 111 citations in OpenAlex.

  1. Is CepA frommSphere · 2025
    Article
  2. Article
  3. Article
  4. In vitro reconstitution of transition metal transporters.The Journal of biological chemistry · 2024
    Review
  5. Article
  6. Article
  7. Review
  8. Metalation and activation of ZnBiophysics reviews · 2023
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Mechanism of Zinc Transport through the Zinc Transporter YiiP.Journal of chemical theory and computation · 2022
    Article
  15. Review
  16. Review
  17. Article
  18. Review
  19. Article
  20. Review

1 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

14 authors at 5 institutions in 1 country.

Nicolas CoudrayLaboratory of Cryo-Electron Microscopy, New York Structural Biology Center, New York, NY 10027, USA.
Salvatore Valvo
Minghui Hu
Ralph Lasala
Changki Kim
Martin Vink
Ming Zhou
Davide Provasi
Marta Filizola
Juoehi Tao
Jia Fang
Pawel A Penczek
Iban Ubarretxena-Belandia
David L Stokes
Icahn School of Medicine at Mount Sinai · USNew York Structural Biology Center · USThe University of Texas Health Science Center at Houston · USNew York University · USColumbia University · US

Funding

Structural Genomics on Membrane ProteinsU54GM095315 · NIGMS · NEW YORK STRUCTURAL BIOLOGY CENTER · PI ROST, BURKHARD · 2010 to 2014
$15.2M
UNIVERSITY OF WASHINGTONU54GM094598 · NIGMS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI STOKES, DAVID L. · 2010 to 2014
$8.3M
Structure and function of urea transportersR01DK088057 · NIDDK · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI ZHOU, MING · 2010 to 2014
$1.7M
Structure and Function of a Phosphorylation Coupled Saccharide TransporterR01GM098878 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI ZHOU, MING · 2011 to 2014
$1.2M
High-throughput Pipeline for Electron CrystallographyR01GM095747 · NIGMS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI STOKES, DAVID L. · 2010 to 2013
$1.2M
NIDDK NIH HHS R01 DK088057NIGMS NIH HHS R01 GM095747NIGMS NIH HHS R01 GM098878NIGMS NIH HHS U54 GM094598NIGMS NIH HHS U54 GM095315NIGMS NIH HHS U54 GM94598
6 · The paper itself

Abstract

YiiP is a dimeric Zn(2+)/H(+) antiporter from Escherichia coli belonging to the cation diffusion facilitator family. We used cryoelectron microscopy to determine a 13-Å resolution structure of a YiiP homolog from Shewanella oneidensis within a lipid bilayer in the absence of Zn(2+). Starting from the X-ray structure in the presence of Zn(2+), we used molecular dynamics flexible fitting to build a model consistent with our map. Comparison of the structures suggests a conformational change that involves pivoting of a transmembrane, four-helix bundle (M1, M2, M4, and M5) relative to the M3-M6 helix pair. Although accessibility of transport sites in the X-ray model indicates that it represents an outward-facing state, our model is consistent with an inward-facing state, suggesting that the conformational change is relevant to the alternating access mechanism for transport. Molecular dynamics simulation of YiiP in a lipid environment was used to address the feasibility of this conformational change. Association of the C-terminal domains is the same in both states, and we speculate that this association is responsible for stabilizing the dimer that, in turn, may coordinate the rearrangement of the transmembrane helices.

Indexed as

Amino Acid SequenceBacterial ProteinsCation Transport ProteinsCryoelectron MicroscopyCrystallography, X-RayModels, MolecularMolecular Dynamics SimulationMolecular Sequence DataProtein ConformationRecombinant ProteinsSequence Homology, Amino AcidShewanellaZincBacterial ProteinsCation Transport ProteinsRecombinant ProteinsZinc

Identifiers

PMID23341604
PMCPMC3568326
OpenAlexW2154740789

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.