IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v5y2014i1d10.1038_ncomms4590.html
   My bibliography  Save this article

Molecular mechanism of Mg2+-dependent gating in CorA

Author

Listed:
  • Olivier Dalmas

    (Institute for Biophysical Dynamics, The University of Chicago)

  • Pornthep Sompornpisut

    (Faculty of Science, Chulalongkorn University)

  • Francisco Bezanilla

    (Institute for Biophysical Dynamics, The University of Chicago)

  • Eduardo Perozo

    (Institute for Biophysical Dynamics, The University of Chicago)

Abstract

CorA is the major transport system responsible for Mg2+ uptake in bacteria and can functionally substitute for its homologue Mrs2p in the yeast inner mitochondrial membrane. Although several CorA crystal structures are available, the molecular mechanism of Mg2+ uptake remains to be established. Here we use electron paramagnetic resonance spectroscopy, electrophysiology and molecular dynamic simulations to show that CorA is regulated by cytoplasmic Mg2+ acting as a ligand and elucidate the basic conformational rearrangements responsible for Mg2+-dependent gating. Mg2+ unbinding at the divalent cation sensor triggers a conformational change that leads to the inward motion of the stalk helix, which propagates to the pore-forming transmembrane helix TM1. Helical tilting and rotation in TM1 generates an iris-like motion that increases the diameter of the permeation pathway, triggering ion conduction. This work establishes the molecular basis of a Mg2+-driven negative feedback loop in CorA as the key physiological event controlling Mg2+ uptake and homeostasis in prokaryotes.

Suggested Citation

  • Olivier Dalmas & Pornthep Sompornpisut & Francisco Bezanilla & Eduardo Perozo, 2014. "Molecular mechanism of Mg2+-dependent gating in CorA," Nature Communications, Nature, vol. 5(1), pages 1-11, May.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms4590
    DOI: 10.1038/ncomms4590
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/ncomms4590
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/ncomms4590?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Louis Tung Faat Lai & Jayashree Balaraman & Fei Zhou & Doreen Matthies, 2023. "Cryo-EM structures of human magnesium channel MRS2 reveal gating and regulatory mechanisms," Nature Communications, Nature, vol. 14(1), pages 1-10, December.
    2. Rangubpit, Warin & Kitjaruwankul, Sunan & Sompornpisut, Pornthep & Pandey, R.B., 2020. "Pinning the conformation of a protein (CorA) in a solute matrix with selective binding," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 556(C).
    3. Ming Li & Yang Li & Yue Lu & Jianhui Li & Xuhang Lu & Yue Ren & Tianlei Wen & Yaojie Wang & Shenghai Chang & Xing Zhang & Xue Yang & Yuequan Shen, 2023. "Molecular basis of Mg2+ permeation through the human mitochondrial Mrs2 channel," Nature Communications, Nature, vol. 14(1), pages 1-11, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms4590. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.