Evidence map›Paper›PMID 24173033›Full record

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

Structures of intermediate transport states of ZneA, a Zn(II)/proton antiporter.

John Edward Pak, Elisabeth Ngonlong Ekendé, Efrem G Kifle, Joseph Daniel O'Connell, Fabien De Angelis, Meseret B Tessema, Kheiro-Mouna Derfoufi, Yaneth Robles-Colmenares, Rebecca A Robbins, Erik Goormaghtigh and 2 more

Abstract 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 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

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

28 citing papers in PubMed.

  1. Article
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  6. Review
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  9. Article
  10. Adaptation ofMicroorganisms · 2021
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. A convenient protein library for spectroscopic calibrations.Computational and structural biotechnology journal · 2020
    Article
  17. MmpL3 is a lipid transporter that binds trehalose monomycolate and phosphatidylethanolamine.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  18. Review
  19. Article
  20. Article
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.

John Edward PakDepartment of Biochemistry and Biophysics, Center for the Structure of Membrane Proteins, Membrane Protein Expression Center, University of California, San Francisco, CA 94158.
Elisabeth Ngonlong Ekendé
Efrem G Kifle
Joseph Daniel O'Connell
Fabien De Angelis
Meseret B Tessema
Kheiro-Mouna Derfoufi
Yaneth Robles-Colmenares
Rebecca A Robbins
Erik Goormaghtigh
Guy Vandenbussche
Robert M Stroud

Funding

Yeast ExpressionP50GM073210 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI STROUD, ROBERT M · 2004 to 2013
$21.5M
Project 6 (Holton)U54GM094625 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI STROUD, ROBERT M · 2010 to 2014
$8.0M
Molecular Basis for Transmembrane Conduction & SignalingR37GM024485 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI STROUD, ROBERT M · 2007 to 2016
$4.7M
NIGMS NIH HHS P50 GM073210NIGMS NIH HHS P50 GM73210NIGMS NIH HHS R37 GM024485NIGMS NIH HHS R37 GM24485NIGMS NIH HHS U54 GM094625
6 · The paper itself

Abstract

Efflux pumps belonging to the ubiquitous resistance-nodulation-cell division (RND) superfamily transport substrates out of cells by coupling proton conduction across the membrane to a conformationally driven pumping cycle. The heavy metal-resistant bacteria Cupriavidus metallidurans CH34 relies notably on as many as 12 heavy metal efflux pumps of the RND superfamily. Here we show that C. metallidurans CH34 ZneA is a proton driven efflux pump specific for Zn(II), and that transport of substrates through the transmembrane domain may be electrogenic. We report two X-ray crystal structures of ZneA in intermediate transport conformations, at 3.0 and 3.7 Å resolution. The trimeric ZneA structures capture protomer conformations that differ in the spatial arrangement and Zn(II) occupancies at a proximal and a distal substrate binding site. Structural comparison shows that transport of substrates through a tunnel that links the two binding sites, toward an exit portal, is mediated by the conformation of a short 14-aa loop. Taken together, the ZneA structures presented here provide mechanistic insights into the conformational changes required for substrate efflux by RND superfamily transporters.

Indexed as

Models, MolecularProtein ConformationProtonsAntiportersBacterial ProteinsBiological TransportCrystallizationCupriavidusX-Ray DiffractionZincAntiportersBacterial ProteinsProtonsZinc

Identifiers

PMID24173033
PMCPMC3832018

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.