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- PDB-7ny1: Structure of the fungal plasma membrane proton pump Pma1 in its a... -
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Basic information
Entry | Database: PDB / ID: 7ny1 | ||||||||||||||||||
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Title | Structure of the fungal plasma membrane proton pump Pma1 in its auto-inhibited state - hexameric assembly | ||||||||||||||||||
![]() | Plasma membrane ATPase | ||||||||||||||||||
![]() | PROTON TRANSPORT / Membrane Protein / P-Type ATPase / proton-transporting ATPase | ||||||||||||||||||
Function / homology | ![]() P-type H+-exporting transporter / proton export across plasma membrane / P-type proton-exporting transporter activity / ATP hydrolysis activity / ATP binding / plasma membrane Similarity search - Function | ||||||||||||||||||
Biological species | ![]() | ||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.26 Å | ||||||||||||||||||
![]() | Heit, S. / Geurts, M.M.G. / Murphy, B.J. / Corey, R. / Mills, D.J. / Kuehlbrandt, W. / Bublitz, M. | ||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Structure of the hexameric fungal plasma membrane proton pump in its autoinhibited state. Authors: Sabine Heit / Maxwell M G Geurts / Bonnie J Murphy / Robin A Corey / Deryck J Mills / Werner Kühlbrandt / Maike Bublitz / ![]() ![]() Abstract: The fungal plasma membrane H-ATPase Pma1 is a vital enzyme, generating a proton-motive force that drives the import of essential nutrients. Autoinhibited Pma1 hexamers in the plasma membrane of ...The fungal plasma membrane H-ATPase Pma1 is a vital enzyme, generating a proton-motive force that drives the import of essential nutrients. Autoinhibited Pma1 hexamers in the plasma membrane of starving fungi are activated by glucose signaling and subsequent phosphorylation of the autoinhibitory domain. As related P-type adenosine triphosphatases (ATPases) are not known to oligomerize, the physiological relevance of Pma1 hexamers remained unknown. We have determined the structure of hexameric Pma1 from by electron cryo-microscopy at 3.3-Å resolution, elucidating the molecular basis for hexamer formation and autoinhibition and providing a basis for structure-based drug development. Coarse-grained molecular dynamics simulations in a lipid bilayer suggest lipid-mediated contacts between monomers and a substantial protein-induced membrane deformation that could act as a proton-attracting funnel. | ||||||||||||||||||
History |
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Structure visualization
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Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 823.9 KB | Display | ![]() |
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PDB format | ![]() | 697 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 819.3 KB | Display | ![]() |
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Full document | ![]() | 889.9 KB | Display | |
Data in XML | ![]() | 129.9 KB | Display | |
Data in CIF | ![]() | 181.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 12644MC ![]() 7nxfC C: citing same article ( M: map data used to model this data |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Components
#1: Protein | Mass: 99984.359 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: A0A0B0DXJ0, P-type H+-exporting transporter #2: Chemical | ChemComp-ADP / #3: Chemical | ChemComp-MG / #4: Chemical | ChemComp-K / Has ligand of interest | N | |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component | Name: Hexameric assembly of the fungal plasma membrane proton pump in its auto-inhibited state Type: COMPLEX / Entity ID: #1 / Source: NATURAL |
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Source (natural) | Organism: ![]() |
Buffer solution | pH: 6.5 |
Specimen | Conc.: 2 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Specimen support | Grid material: COPPER / Grid mesh size: 400 divisions/in. / Grid type: C-flat-2/2 |
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 70 % / Chamber temperature: 283 K |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD |
Image recording | Electron dose: 42 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
Software | Name: PHENIX / Version: 1.18.2_3874: / Classification: refinement | ||||||||||||||||||||||||
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EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
Symmetry | Point symmetry: C6 (6 fold cyclic) | ||||||||||||||||||||||||
3D reconstruction | Resolution: 3.26 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 59511 / Symmetry type: POINT | ||||||||||||||||||||||||
Refine LS restraints |
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