1MHS
Model of Neurospora crassa proton ATPase
Summary for 1MHS
| Entry DOI | 10.2210/pdb1mhs/pdb |
| Related | 1eul 1iwo |
| Descriptor | Plasma Membrane ATPase (1 entity in total) |
| Functional Keywords | ion transport, proton pump, membrane protein, p-type atpase, active transport, proton transport |
| Biological source | Neurospora crassa |
| Total number of polymer chains | 2 |
| Total formula weight | 199968.72 |
| Authors | Kuhlbrandt, W. (deposition date: 2002-08-21, release date: 2002-09-18, Last modification date: 2024-02-14) |
| Primary citation | Kuhlbrandt, W.,Zeelen, J.,Dietrich, J. Structure, mechanism and regulation of the Neurospora plasma membrane H+-ATPase Science, 297:1692-1696, 2002 Cited by PubMed 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. PubMed: 12169656DOI: 10.1126/science.1072574 PDB entries with the same primary citation |
| Experimental method | ELECTRON CRYSTALLOGRAPHY (8 Å) |
Structure validation
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