Evidence map›Paper›PMID 20637423›Full record

ArticleStructure (London, England : 1993)2010

Structural dynamics of the magnesium-bound conformation of CorA in a lipid bilayer.

Olivier Dalmas, Luis G Cuello, Vishwanath Jogini, D Marien Cortes, Benoit Roux, Eduardo Perozo

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Conformational ensembles of the magnesium channel CorA reveal structural basis for channel gating.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Loss of cytosolic MgBiochimica et biophysica acta. General subjects · 2019
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. A repulsion mechanism explains magnesium permeation and selectivity in CorA.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  13. Structural insights into the mechanisms of Mg2+ uptake, transport, and gating by CorA.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  14. Article
  15. Article
  16. Article
  17. Mg2+ channel selectivity probed by EPR.Structure (London, England : 1993) · 2010
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Olivier DalmasDepartment of Biochemistry and Molecular Biology, Institute for Biophysical Dynamics, The University of Chicago, IL 60637, USA.
Luis G Cuello
Vishwanath Jogini
D Marien Cortes
Benoit Roux
Eduardo Perozo

Funding

Computational Studies of Ion Channels - Resubmission 01R01GM062342 · NIGMS · WEILL MEDICAL COLLEGE OF CORNELL UNIV · PI ROUX, BENOIT · 2001 to 2022
$8.7M
Structural basis for transmembrane Mg2+ transportR01GM088406 · NIGMS · UNIVERSITY OF CHICAGO · PI PEROZO, EDUARDO A · 2009 to 2012
$1.3M
NIGMS NIH HHS R01 GM062342NIGMS NIH HHS R01 GM088406
6 · The paper itself

Abstract

The transmembrane conformation of Thermotoga maritima CorA, a magnesium transport system, has been studied in its Mg(2+)-bound form by site-directed spin labeling and electron paramagnetic resonance spectroscopy. Probe mobility together with accessibility data were used to evaluate the overall dynamics and relative arrangement of individual transmembrane segments TM1 and TM2. TM1 extends toward the cytoplasmic side creating a water-filled cavity, while TM2 is located in the periphery of the oligomer, contacting the lipid bilayer. A structural model for the conserved extracellular loop was generated based on EPR data and MD simulations, in which residue E316 is located toward the five-fold symmetry axis in position to electrostatically influence divalent ion translocation. Electrostatic analysis of our model suggest that, in agreement with the crystal structure, Mg(2+) -bound CorA is in a closed conformation. The present results suggest that long-range structural rearrangements are necessary to allow Mg(2+) translocation.

Indexed as

Models, MolecularProtein ConformationCation Transport ProteinsEdetic AcidElectron Spin Resonance SpectroscopyLipid BilayersMagnesiumOxygenSpin LabelsStatic ElectricityThermotoga maritimaCation Transport ProteinsEDDAEdetic AcidLipid BilayersMagnesiumOxygenSpin Labels

Identifiers

PMID20637423
PMCPMC2935691

What OpenQuestion holds

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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.