ArticleThe Journal of biological chemistry2009
Ligand binding in the conserved interhelical loop of CorA, a magnesium transporter from Mycobacterium tuberculosis.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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.
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.
Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- Ion selectivity and gating behavior of the CorA-type channel Bpss1228.Frontiers in chemistry · 2022Article
- Cation permeability in CorA family of proteins.Scientific reports · 2020Article
- Article
- Loss of cytosolic MgBiochimica et biophysica acta. General subjects · 2019Article
- Iron Acquisition in Mycobacterium avium subsp. paratuberculosis.Journal of bacteriology · 2015Article
- Structural asymmetry in the magnesium channel CorA points to sequential allosteric regulation.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Article
- Drug sensitivity, drug-resistant mutations, and structures of three conductance domains of viral porins.Biochimica et biophysica acta · 2011Review
- Article
- Article
- Structural dynamics of the magnesium-bound conformation of CorA in a lipid bilayer.Structure (London, England : 1993) · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
CorA is a constitutively expressed magnesium transporter in many bacteria. The crystal structures of Thermotoga maritima CorA provide an excellent structural framework for continuing studies. Here, the ligand binding properties of the conserved interhelical loop, the only portion of the protein exposed to the periplasmic space, are characterized by solution nuclear magnetic resonance spectroscopy. Through titration experiments performed on the isolated transmembrane domain of Mycobacterium tuberculosis CorA, it was found that two CorA substrates (Mg2+ and Co2+) and the CorA-specific inhibitor (Co(III) hexamine chloride) bind in the loop at the same binding site. This site includes the glutamic acid residue from the conserved "MPEL" motif. The relatively large dissociation constants indicate that such interactions are weak but not atypical for channels. The present data support the hypothesis that the negatively charged loop could act as an electrostatic ring, increasing local substrate concentrations before transport across the membrane.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.