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TitleStructure, mechanism, and regulation of the Neurospora plasma membrane H+-ATPase.
Journal, issue, pagesScience, Vol. 297, Issue 5587, Page 1692-1696, Year 2002
Publish dateSep 6, 2002
AuthorsWerner Kühlbrandt / Johan Zeelen / Jens Dietrich /
PubMed AbstractProton pumps in the plasma membrane of plants and yeasts maintain the intracellular pH and membrane potential. To gain insight into the molecular mechanisms of proton pumping, we built an atomic ...Proton pumps in the plasma membrane of plants and yeasts maintain the intracellular pH and membrane potential. To gain insight into the molecular mechanisms of proton pumping, we built an atomic homology model of the proton pump based on the 2.6 angstrom x-ray structure of the related Ca2+ pump from rabbit sarcoplasmic reticulum. The model, when fitted to an 8 angstrom map of the Neurospora proton pump determined by electron microscopy, reveals the likely path of the proton through the membrane and shows that the nucleotide-binding domain rotates by approximately 70 degrees to deliver adenosine triphosphate (ATP) to the phosphorylation site. A synthetic peptide corresponding to the carboxyl-terminal regulatory domain stimulates ATPase activity, suggesting a mechanism for proton transport regulation.
External linksScience / PubMed:12169656
MethodsEM (electron crystallography)
Resolution8 Å
Structure data

PDB-1mhs:
Model of Neurospora crassa proton ATPase
Method: ELECTRON CRYSTALLOGRAPHY / Resolution: 8.0 Å

Source
  • neurospora crassa (fungus)
KeywordsMEMBRANE PROTEIN / PROTON TRANSPORT / ion transport / proton pump / P-type ATPase / active transport

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