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Open data
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Basic information
| Entry | Database: PDB / ID: 9moy | |||||||||||||||
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| Title | Reconstituted yeast V-ATPase bound to Rtc5p | |||||||||||||||
Components |
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Keywords | HYDROLASE / Vacuolar ATPase / proton pump / Rtc5p / membrane protein | |||||||||||||||
| Function / homology | Function and homology informationvacuole-mitochondrion membrane contact site / cell wall mannoprotein biosynthetic process / ATPase-coupled ion transmembrane transporter activity / protein localization to vacuolar membrane / cellular response to alkaline pH / proton-transporting V-type ATPase, V1 domain / Insulin receptor recycling / Transferrin endocytosis and recycling / polyphosphate metabolic process / ROS and RNS production in phagocytes ...vacuole-mitochondrion membrane contact site / cell wall mannoprotein biosynthetic process / ATPase-coupled ion transmembrane transporter activity / protein localization to vacuolar membrane / cellular response to alkaline pH / proton-transporting V-type ATPase, V1 domain / Insulin receptor recycling / Transferrin endocytosis and recycling / polyphosphate metabolic process / ROS and RNS production in phagocytes / Amino acids regulate mTORC1 / Golgi lumen acidification / proteasome storage granule assembly / P-type proton-exporting transporter activity / vacuolar transport / vacuolar proton-transporting V-type ATPase, V1 domain / vacuolar proton-transporting V-type ATPase, V0 domain / endosomal lumen acidification / vacuole organization / protein targeting to vacuole / proton-transporting V-type ATPase complex / fungal-type vacuole / pexophagy / vacuolar proton-transporting V-type ATPase complex / cellular hyperosmotic response / vacuolar acidification / fungal-type vacuole membrane / phosphatidylinositol-3,5-bisphosphate binding / proton transmembrane transporter activity / proton-transporting ATPase activity, rotational mechanism / intracellular copper ion homeostasis / H+-transporting two-sector ATPase / ATP metabolic process / RNA endonuclease activity / Neutrophil degranulation / proton transmembrane transport / cell periphery / transmembrane transport / endocytosis / cytoplasmic stress granule / intracellular calcium ion homeostasis / ATPase binding / protein-containing complex assembly / response to oxidative stress / intracellular iron ion homeostasis / membrane raft / Golgi membrane / endoplasmic reticulum membrane / ATP hydrolysis activity / ATP binding / membrane / nucleus / cytoplasm Similarity search - Function | |||||||||||||||
| Biological species | ![]() | |||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.6 Å | |||||||||||||||
Authors | Wilkens, S. / Khan, M.M. | |||||||||||||||
| Funding support | United States, 1items
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Citation | Journal: To Be PublishedTitle: TLDc Protein Rtc5p Assembles Yeast V-ATPase Authors: Wilkens, S. / Khan, M.M. | |||||||||||||||
| 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 | 9moy.cif.gz | 3.3 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9moy.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9moy.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mo/9moy ftp://data.pdbj.org/pub/pdb/validation_reports/mo/9moy | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 48491MC ![]() 9nn1C C: citing same article ( M: map data used to model this data |
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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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Components
-Protein , 4 types, 6 molecules ACERef
| #1: Protein | Mass: 67796.508 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: B3LH69, H+-transporting two-sector ATPase #7: Protein | | Mass: 64368.312 Da / Num. of mol.: 1 / Mutation: N-terminal 6xHis-tag Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: RTC5, SCRG_01514 / Production host: ![]() #13: Protein | | Mass: 29694.885 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #14: Protein | | Mass: 9369.934 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-V-type proton ATPase subunit ... , 13 types, 26 molecules GIKHJLMNOSTUVWXYZabcdBDFPQ
| #2: Protein | Mass: 26508.393 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() #3: Protein | Mass: 12738.706 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() #4: Protein | | Mass: 29235.023 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #5: Protein | | Mass: 13479.170 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #6: Protein | | Mass: 44241.352 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #8: Protein | | Mass: 39822.484 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #9: Protein | | Mass: 22610.641 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #10: Protein | | Mass: 17046.361 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #11: Protein | Mass: 16357.501 Da / Num. of mol.: 8 / Source method: isolated from a natural source / Source: (natural) ![]() #12: Protein | | Mass: 8387.065 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #15: Protein | Mass: 57815.023 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() #16: Protein | | Mass: 54482.609 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #17: Protein | | Mass: 95625.484 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Non-polymers , 1 types, 1 molecules 
| #18: Chemical | ChemComp-ADP / |
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-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: Reconstituted yeast V-ATPase bound to Rtc5p / Type: COMPLEX / Entity ID: #1-#17 / Source: NATURAL |
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| Molecular weight | Value: 1.1 MDa / Experimental value: NO |
| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 7.4 |
| 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: 300 divisions/in. / Grid type: C-flat-1.2/1.3 |
| Vitrification | Instrument: LEICA EM GP / Cryogen name: ETHANE / Humidity: 90 % / Chamber temperature: 279 K / Details: Leica EM GP2 |
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Electron microscopy imaging
| Microscopy | Model: TFS GLACIOS |
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| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 92000 X / Nominal defocus max: 2000 nm / Nominal defocus min: 400 nm / Cs: 2.7 mm |
| Image recording | Average exposure time: 5.82 sec. / Electron dose: 52.5 e/Å2 / Film or detector model: TFS FALCON 4i (4k x 4k) / Num. of real images: 7819 |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||
| Particle selection | Num. of particles selected: 332570 | ||||||||||||||||||||||||||||||||||||
| Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.6 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 90977 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||||||
| Atomic model building | 3D fitting-ID: 1
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| Refinement | Cross valid method: NONE Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2 | ||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 118.71 Å2 | ||||||||||||||||||||||||||||||||||||
| Refine LS restraints |
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