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  Structure, mechanism, and regulation of the Neurospora plasma membrane H+-ATPase

Kühlbrandt, W., Zeelen, J., & Dietrich, J. (2002). Structure, mechanism, and regulation of the Neurospora plasma membrane H+-ATPase. Science, 297(5587), 1692-1696. doi:10.1126/science.1072574.

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 Creators:
Kühlbrandt, Werner1, Author           
Zeelen, Johan1, Author           
Dietrich, Jens1, Author           
Affiliations:
1Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              

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Free keywords: Amino Acid Sequence ; Cell Membrane/ch [Chemistry] ; Cell Membrane/en [Enzymology] ; Cryoelectron Microscopy ; Enzyme Activation ; Models, Molecular ; Molecular Sequence Data ; *Neurospora/en [Enzymology] ; Peptide Fragments/me [Metabolism] ; Protein Conformation ; Protein Structure, Tertiary ; *Proton-Translocating ATPases/ch [Chemistry] ; Proton-Translocating ATPases/me [Metabolism]
 Abstract: 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.

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Language(s): eng - English
 Dates: 2002-04-052002-07-252002-08-082002-09-06
 Publication Status: Published in print
 Pages: 5
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1126/science.1072574
PMID: 12169656
 Degree: -

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Title: Science
  Abbreviation : Science
Source Genre: Journal
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Publ. Info: Washington, D.C. : American Association for the Advancement of Science
Pages: - Volume / Issue: 297 (5587) Sequence Number: - Start / End Page: 1692 - 1696 Identifier: ISSN: 0036-8075
CoNE: https://pure.mpg.de/cone/journals/resource/991042748276600_1