ArticleThe Journal of biological chemistry2012
The periplasmic loop provides stability to the open state of the CorA magnesium channel.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed, 16 citations in OpenAlex.
- Asymmetric CorA Gating Mechanism as Observed by Molecular Dynamics Simulations.Journal of chemical information and modeling · 2021Article
- Article
- Loss of cytosolic MgBiochimica et biophysica acta. General subjects · 2019Article
- A repulsion mechanism explains magnesium permeation and selectivity in CorA.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Functional fragments of disorder in outer membrane β barrel proteins.Intrinsically disordered proteinsArticle
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Authors and funding
3 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Crystal structures of the CorA Mg(2+) channel have suggested that metal binding in the cytoplasmic domain stabilizes the pentamer in a closed conformation. The open "metal free" state of the channel is, however, still structurally uncharacterized. Here, we have attempted to map conformational states of CorA from Thermotoga maritima by determining which residues support the pentameric structure in the presence or absence of Mg(2+). We find that when Mg(2+) is present, the pentamer is stabilized by the putative gating sites (M1/M2) in the cytoplasmic domain. Strikingly however, we find that the conserved and functionally important periplasmic loop is vital for the integrity of the pentamer when Mg(2+) is absent from the M1/M2 sites. Thus, although the periplasmic loops were largely disordered in the x-ray structures of the closed channel, our data suggests a prominent role for the loops in stabilizing the open conformation of the CorA channels.
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