Back to Search
Start Over
Structure, mechanism, and regulation of the Neurospora plasma membrane H+-ATPase.
- Source :
-
Science (New York, N.Y.) [Science] 2002 Sep 06; Vol. 297 (5587), pp. 1692-6. Date of Electronic Publication: 2002 Aug 08. - Publication Year :
- 2002
-
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.
- Subjects :
- Amino Acid Sequence
Cell Membrane chemistry
Cell Membrane enzymology
Cryoelectron Microscopy
Enzyme Activation
Models, Molecular
Molecular Sequence Data
Peptide Fragments metabolism
Protein Conformation
Protein Structure, Tertiary
Proton-Translocating ATPases metabolism
Neurospora enzymology
Proton-Translocating ATPases chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1095-9203
- Volume :
- 297
- Issue :
- 5587
- Database :
- MEDLINE
- Journal :
- Science (New York, N.Y.)
- Publication Type :
- Academic Journal
- Accession number :
- 12169656
- Full Text :
- https://doi.org/10.1126/science.1072574