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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | Complete V1 Complex from Saccharomyces cerevisiae | |||||||||
Map data | Complete V1 Complex | |||||||||
Sample |
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Keywords | V-ATPase / HYDROLASE | |||||||||
| Function / homology | Function and homology informationproton-transporting V-type ATPase, V1 domain / Insulin receptor recycling / Transferrin endocytosis and recycling / ROS and RNS production in phagocytes / Amino acids regulate mTORC1 / Golgi lumen acidification / proton-transporting two-sector ATPase complex, catalytic domain / vacuolar proton-transporting V-type ATPase, V1 domain / endosomal lumen acidification / proton-transporting V-type ATPase complex ...proton-transporting V-type ATPase, V1 domain / Insulin receptor recycling / Transferrin endocytosis and recycling / ROS and RNS production in phagocytes / Amino acids regulate mTORC1 / Golgi lumen acidification / proton-transporting two-sector ATPase complex, catalytic domain / vacuolar proton-transporting V-type ATPase, V1 domain / endosomal lumen acidification / proton-transporting V-type ATPase complex / vacuolar proton-transporting V-type ATPase complex / vacuolar acidification / fungal-type vacuole membrane / proton-transporting ATPase activity, rotational mechanism / ATP metabolic process / proton transmembrane transport / Golgi membrane / ATP binding Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.5 Å | |||||||||
Authors | Vasanthakumar T / Keon KA | |||||||||
| Funding support | Canada, 1 items
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Citation | Journal: Nat Struct Mol Biol / Year: 2022Title: Coordinated conformational changes in the V complex during V-ATPase reversible dissociation. Authors: Thamiya Vasanthakumar / Kristine A Keon / Stephanie A Bueler / Michael C Jaskolka / John L Rubinstein / ![]() Abstract: Vacuolar-type ATPases (V-ATPases) are rotary enzymes that acidify intracellular compartments in eukaryotic cells. These multi-subunit complexes consist of a cytoplasmic V region that hydrolyzes ATP ...Vacuolar-type ATPases (V-ATPases) are rotary enzymes that acidify intracellular compartments in eukaryotic cells. These multi-subunit complexes consist of a cytoplasmic V region that hydrolyzes ATP and a membrane-embedded V region that transports protons. V-ATPase activity is regulated by reversible dissociation of the two regions, with the isolated V and V complexes becoming autoinhibited on disassembly and subunit C subsequently detaching from V. In yeast, assembly of the V and V regions is mediated by the regulator of the ATPase of vacuoles and endosomes (RAVE) complex through an unknown mechanism. We used cryogenic-electron microscopy of yeast V-ATPase to determine structures of the intact enzyme, the dissociated but complete V complex and the V complex lacking subunit C. On separation, V undergoes a dramatic conformational rearrangement, with its rotational state becoming incompatible for reassembly with V. Loss of subunit C allows V to match the rotational state of V, suggesting how RAVE could reassemble V and V by recruiting subunit C. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_25996.map.gz | 7.4 MB | EMDB map data format | |
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| Header (meta data) | emd-25996-v30.xml emd-25996.xml | 23.6 KB 23.6 KB | Display Display | EMDB header |
| Images | emd_25996.png | 103.8 KB | ||
| Filedesc metadata | emd-25996.cif.gz | 7.8 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-25996 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-25996 | HTTPS FTP |
-Validation report
| Summary document | emd_25996_validation.pdf.gz | 363.6 KB | Display | EMDB validaton report |
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| Full document | emd_25996_full_validation.pdf.gz | 363.1 KB | Display | |
| Data in XML | emd_25996_validation.xml.gz | 7.3 KB | Display | |
| Data in CIF | emd_25996_validation.cif.gz | 8.4 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-25996 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-25996 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 7tmmMC ![]() 7tmoC ![]() 7tmpC ![]() 7tmqC ![]() 7tmrC ![]() 7tmsC ![]() 7tmtC C: citing same article ( M: atomic model generated by this map |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_25996.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Complete V1 Complex | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.03 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
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Sample components
+Entire : Complete V1 Complex
+Supramolecule #1: Complete V1 Complex
+Macromolecule #1: H(+)-transporting two-sector ATPase
+Macromolecule #2: Vacuolar proton pump subunit B
+Macromolecule #3: V-ATPase subunit E
+Macromolecule #4: V-type proton ATPase subunit G
+Macromolecule #5: V-type proton ATPase subunit D
+Macromolecule #6: V-type proton ATPase subunit F
+Macromolecule #7: V-type proton ATPase subunit C
+Macromolecule #8: V-type proton ATPase subunit H
+Macromolecule #9: ADENOSINE-5'-DIPHOSPHATE
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.4 |
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| Vitrification | Cryogen name: ETHANE-PROPANE |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 43.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.5 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Authors
Canada, 1 items
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Processing
FIELD EMISSION GUN
