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Yorodumi- PDB-36qx: Arabidopsis thaliana V-type ATPase, State 1 bound to OXR5, Backbo... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 36qx | |||||||||
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| Title | Arabidopsis thaliana V-type ATPase, State 1 bound to OXR5, Backbone model | |||||||||
Components |
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Keywords | HYDROLASE / Membrane protein / protein complex / pH regulation | |||||||||
| Function / homology | Function and homology informationtrans-Golgi network transport vesicle membrane / proton-transporting V-type ATPase complex assembly / plant-type cell wall biogenesis / proton-transporting two-sector ATPase complex / unidimensional cell growth / glucose mediated signaling pathway / plant-type vacuole membrane / proton-transporting V-type ATPase, V1 domain / proton-transporting two-sector ATPase complex, catalytic domain / lysosomal lumen acidification ...trans-Golgi network transport vesicle membrane / proton-transporting V-type ATPase complex assembly / plant-type cell wall biogenesis / proton-transporting two-sector ATPase complex / unidimensional cell growth / glucose mediated signaling pathway / plant-type vacuole membrane / proton-transporting V-type ATPase, V1 domain / proton-transporting two-sector ATPase complex, catalytic domain / lysosomal lumen acidification / pollen development / proton-transporting V-type ATPase, V0 domain / plant-type cell wall / embryo development ending in seed dormancy / proton-transporting V-type ATPase complex / vacuolar proton-transporting V-type ATPase, V1 domain / vacuolar transport / vacuolar proton-transporting V-type ATPase, V0 domain / negative regulation of actin filament depolymerization / vacuolar proton-transporting V-type ATPase complex / plasmodesma / plant-type vacuole / chloroplast envelope / vacuolar acidification / actin filament capping / vacuole / vacuolar membrane / Golgi organization / proton-transporting ATPase activity, rotational mechanism / actin filament bundle assembly / H+-transporting two-sector ATPase / ATP metabolic process / response to cold / proton-transporting ATP synthase activity, rotational mechanism / proton transmembrane transport / trans-Golgi network membrane / trans-Golgi network / chloroplast / cytoplasmic stress granule / cytosolic ribosome / actin filament binding / ATPase binding / protease binding / endosome / structural constituent of ribosome / Golgi membrane / regulation of transcription by RNA polymerase II / endoplasmic reticulum membrane / Golgi apparatus / ATP hydrolysis activity / protein-containing complex / mitochondrion / extracellular region / ATP binding / membrane / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.3 Å | |||||||||
Authors | Khamina, M. / Rubinstein, J.L. | |||||||||
| Funding support | Canada, Germany, 2items
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Citation | Journal: To Be PublishedTitle: Cryo-EM structure of the Arabidopsis thaliana V-type ATPase Authors: Khamina, M. / Wunsch, N. / Lupanga, U. / Fink, F. / Wang, H. / Schulze, W.X. / Schumacher, K. / Rubinstein, J.L. | |||||||||
| History |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 36qx.cif.gz | 1.1 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb36qx.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 36qx.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/6q/36qx ftp://data.pdbj.org/pub/pdb/validation_reports/6q/36qx | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 77789MC ![]() 36quC ![]() 36qvC ![]() 36qwC ![]() 77756 ![]() 77757 ![]() 77766 ![]() 77767 ![]() 77774 M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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Components
-Protein , 2 types, 4 molecules TCEA
| #1: Protein | Mass: 59973.324 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #15: Protein | Mass: 68884.234 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: O23654, H+-transporting two-sector ATPase |
-V-type proton ATPase subunit ... , 14 types, 28 molecules aFDBGIKHJLMNPbcdeghijklmnorO
| #2: Protein | Mass: 93512.727 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() | ||||||||||||||||||||||||
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| #3: Protein | Mass: 54164.352 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() #4: Protein | Mass: 26101.053 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() #5: Protein | Mass: 12416.915 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() #6: Protein | | Mass: 29104.756 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #7: Protein | | Mass: 14276.354 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #8: Protein | | Mass: 50346.262 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #9: Protein | | Mass: 35015.453 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #10: Protein | | Mass: 18383.625 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #11: Protein | | Mass: 40835.688 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #12: Protein | | Mass: 7688.377 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #13: Protein | Mass: 16581.588 Da / Num. of mol.: 9 / Source method: isolated from a natural source / Source: (natural) ![]() #14: Protein | | Mass: 39164.426 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #16: Protein | | Mass: 42667.199 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Non-polymers , 2 types, 2 molecules 


| #17: Chemical | ChemComp-ADP / |
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| #18: Chemical | ChemComp-MG / |
-Details
| Has ligand of interest | Y |
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| Has protein modification | N |
-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: Arabidopsis V-ATPase State 1 / Type: COMPLEX / Entity ID: #1-#16 / Source: NATURAL |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 7 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid material: COPPER/RHODIUM / Grid mesh size: 400 divisions/in. / Grid type: Homemade |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 130000 X / Nominal defocus max: 2000 nm / Nominal defocus min: 800 nm |
| Image recording | Electron dose: 40 e/Å2 / Film or detector model: TFS FALCON 4i (4k x 4k) / Num. of real images: 7681 |
| EM imaging optics | Energyfilter name: TFS Selectris X / Energyfilter slit width: 10 eV |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||
| Particle selection | Num. of particles selected: 190490 | ||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 4.3 Å / Resolution method: DIFFRACTION PATTERN/LAYERLINES / Num. of particles: 5323 / Symmetry type: POINT | ||||||||||||||||||||||||||||
| Refinement | Highest resolution: 4.3 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||||||
| Refine LS restraints |
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