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Open data
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Basic information
| Entry | Database: PDB / ID: 9cop | ||||||||||||||||||||||||||||||||||||
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| Title | Yeast RAVE bound to V-ATPase V1 complex | ||||||||||||||||||||||||||||||||||||
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Keywords | HYDROLASE / V-ATPase / RAVE / assembly | ||||||||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationRAVE complex / Iron uptake and transport / CBF3 complex / regulation of transcription by galactose / : / cellular response to methylmercury / vacuolar proton-transporting V-type ATPase complex assembly / vacuole-mitochondrion membrane contact site / septin ring assembly / Insulin receptor recycling ...RAVE complex / Iron uptake and transport / CBF3 complex / regulation of transcription by galactose / : / cellular response to methylmercury / vacuolar proton-transporting V-type ATPase complex assembly / vacuole-mitochondrion membrane contact site / septin ring assembly / Insulin receptor recycling / Transferrin endocytosis and recycling / ROS and RNS production in phagocytes / Amino acids regulate mTORC1 / Golgi lumen acidification / proteasome storage granule assembly / vacuolar proton-transporting V-type ATPase, V1 domain / early endosome to late endosome transport / endosomal lumen acidification / regulation of exit from mitosis / proton-transporting V-type ATPase complex / kinetochore assembly / pexophagy / intron homing / intein-mediated protein splicing / vacuolar proton-transporting V-type ATPase complex / exit from mitosis / positive regulation of D-glucose transmembrane transport / vacuolar acidification / protein neddylation / fungal-type vacuole membrane / mitotic intra-S DNA damage checkpoint signaling / mitochondrial fusion / silent mating-type cassette heterochromatin formation / regulation of metabolic process / SCF ubiquitin ligase complex / SCF-dependent proteasomal ubiquitin-dependent protein catabolic process / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / Orc1 removal from chromatin / cullin family protein binding / Antigen processing: Ubiquitination & Proteasome degradation / DNA replication origin binding / proton-transporting ATPase activity, rotational mechanism / regulation of protein-containing complex assembly / subtelomeric heterochromatin formation / H+-transporting two-sector ATPase / ATP metabolic process / negative regulation of cytoplasmic translation / Neutrophil degranulation / endomembrane system / proton transmembrane transport / regulation of mitotic cell cycle / G1/S transition of mitotic cell cycle / kinetochore / transmembrane transport / G2/M transition of mitotic cell cycle / intracellular calcium ion homeostasis / cytoplasmic stress granule / protein transport / mitotic cell cycle / protein-containing complex assembly / ubiquitin-dependent protein catabolic process / early endosome membrane / endonuclease activity / Hydrolases; Acting on ester bonds / chromosome, telomeric region / protein ubiquitination / membrane raft / Golgi membrane / mRNA binding / ATP hydrolysis activity / DNA binding / ATP binding / nucleus / membrane / cytoplasm Similarity search - Function | ||||||||||||||||||||||||||||||||||||
| Biological species | ![]() | ||||||||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.7 Å | ||||||||||||||||||||||||||||||||||||
Authors | Wang, H. / Rubinstein, J.L. | ||||||||||||||||||||||||||||||||||||
| Funding support | United States, Canada, 2items
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Citation | Journal: Proc Natl Acad Sci U S A / Year: 2024Title: Structure of yeast RAVE bound to a partial V complex. Authors: Hanlin Wang / Maureen Tarsio / Patricia M Kane / John L Rubinstein / ![]() Abstract: Vacuolar-type ATPases (V-ATPases) are membrane-embedded proton pumps that acidify intracellular compartments in almost all eukaryotic cells. Homologous with ATP synthases, these multisubunit enzymes ...Vacuolar-type ATPases (V-ATPases) are membrane-embedded proton pumps that acidify intracellular compartments in almost all eukaryotic cells. Homologous with ATP synthases, these multisubunit enzymes consist of a soluble catalytic V subcomplex and a membrane-embedded proton-translocating V subcomplex. The V and V subcomplexes can undergo reversible dissociation to regulate proton pumping, with reassociation of V and V requiring the protein complex known as RAVE (regulator of the ATPase of vacuoles and endosomes). In the yeast , RAVE consists of subunits Rav1p, Rav2p, and Skp1p. We used electron cryomicroscopy (cryo-EM) to determine a structure of yeast RAVE bound to V. In the structure, RAVE is an L-shaped complex with Rav2p pointing toward the membrane and Skp1p distant from both the membrane and V. Only Rav1p interacts with V, binding to a region of subunit A not found in the corresponding ATP synthase subunit. When bound to RAVE, V is in a rotational state suitable for binding the free V complex, but in the structure, it is partially disrupted, missing five of its 16 subunits. Other than these missing subunits and the conformation of the inhibitory subunit H, the V complex with RAVE appears poised for reassembly with V. | ||||||||||||||||||||||||||||||||||||
| 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 | 9cop.cif.gz | 1.5 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9cop.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9cop.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9cop_validation.pdf.gz | 1 MB | Display | wwPDB validaton report |
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| Full document | 9cop_full_validation.pdf.gz | 1 MB | Display | |
| Data in XML | 9cop_validation.xml.gz | 121.5 KB | Display | |
| Data in CIF | 9cop_validation.cif.gz | 199.5 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/co/9cop ftp://data.pdbj.org/pub/pdb/validation_reports/co/9cop | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 45788MC 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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Components
-Protein , 2 types, 3 molecules AEz
| #1: Protein | Mass: 118782.547 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: P17255, H+-transporting two-sector ATPase #10: Protein | | Mass: 22357.270 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-V-type proton ATPase subunit ... , 6 types, 9 molecules BFIKJLMNP
| #2: Protein | Mass: 57815.023 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #3: Protein | Mass: 26508.393 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #4: Protein | Mass: 12738.706 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #5: Protein | | Mass: 29235.023 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #6: Protein | | Mass: 13347.975 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #7: Protein | | Mass: 54482.609 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Regulator of V-ATPase in vacuolar membrane protein ... , 2 types, 2 molecules xy
| #8: Protein | Mass: 155127.328 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #9: Protein | Mass: 40061.035 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Non-polymers , 2 types, 4 molecules 


| #11: Chemical | | #12: Chemical | |
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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: Yeast RAVE bound to V-ATPase V1 complex / Type: COMPLEX / Entity ID: #1-#10 / Source: NATURAL |
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| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 7.4 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid material: COPPER/RHODIUM / Grid type: Homemade |
| Vitrification | Instrument: LEICA EM GP / 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: FEI TITAN KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2300 nm / Nominal defocus min: 500 nm |
| Image recording | Electron dose: 42 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
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Processing
| EM software | Name: PHENIX / Category: model refinement |
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
| 3D reconstruction | Resolution: 2.7 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 71341 / Symmetry type: POINT |
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Canada, 2items
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FIELD EMISSION GUN