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TitleConformations of NhaA, the Na/H exchanger from Escherichia coli, in the pH-activated and ion-translocating states.
Journal, issue, pagesJ Mol Biol, Vol. 386, Issue 2, Page 351-365, Year 2009
Publish dateFeb 20, 2009
AuthorsMatthias Appel / Dilem Hizlan / Kutti R Vinothkumar / Christine Ziegler / Werner Kühlbrandt /
PubMed AbstractNhaA, the main sodium-proton exchanger in the inner membrane of Escherichia coli, regulates the cytosolic concentrations of H and Na. It is inactive at acidic pH, becomes active between pH 6 and pH ...NhaA, the main sodium-proton exchanger in the inner membrane of Escherichia coli, regulates the cytosolic concentrations of H and Na. It is inactive at acidic pH, becomes active between pH 6 and pH 7, and reaches maximum activity at pH 8. By cryo-electron microscopy of two-dimensional crystals grown at pH 4 and incubated at higher pH, we identified two sequential conformational changes in the protein in response to pH or substrate ions. The first change is induced by a rise in pH from 6 to 7 and marks the transition from the inactive state to the pH-activated state. pH activation, which precedes the ion-induced conformational change, is accompanied by an overall expansion of the NhaA monomer and a local ordering of the N-terminus. The second conformational change is induced by the substrate ions Na and Li at pH above 7 and involves a 7-A displacement of helix IVp. This movement would cause a charge imbalance at the ion-binding site that may trigger the release of the substrate ion and open a periplasmic exit channel.
External linksJ Mol Biol / PubMed:19135453
MethodsEM (electron crystallography)
Resolution7 Å
Structure data

PDB-3fi1:
NhaA dimer model
Method: ELECTRON CRYSTALLOGRAPHY / Resolution: 7.0 Å

Source
  • escherichia coli k-12 (bacteria)
KeywordsMEMBRANE PROTEIN / membrane protein sodium proton antiporter / Antiport / Cell inner membrane / Cell membrane / Ion transport / Membrane / Sodium transport / Transmembrane / Transport

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