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Open data
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Basic information
| Entry | Database: PDB / ID: 8qx8 | |||||||||||||||||||||||||||
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| Title | Endosomal membrane tethering complex CORVET | |||||||||||||||||||||||||||
Components |
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Keywords | ENDOCYTOSIS / CORVET / membrane fusion / endosome / Rab GTPase / tethering | |||||||||||||||||||||||||||
| Function / homology | Function and homology informationhistone catabolic process / organelle fusion / CORVET complex / HOPS complex / endosomal vesicle fusion / vesicle tethering / regulation of vacuole fusion, non-autophagic / vacuole inheritance / Golgi to vacuole transport / regulation of SNARE complex assembly ...histone catabolic process / organelle fusion / CORVET complex / HOPS complex / endosomal vesicle fusion / vesicle tethering / regulation of vacuole fusion, non-autophagic / vacuole inheritance / Golgi to vacuole transport / regulation of SNARE complex assembly / vesicle fusion with vacuole / vacuole fusion, non-autophagic / Golgi to endosome transport / late endosome to vacuole transport via multivesicular body sorting pathway / vesicle docking / vacuole organization / protein targeting to vacuole / late endosome to vacuole transport / endosome organization / piecemeal microautophagy of the nucleus / fungal-type vacuole / vacuolar acidification / Golgi stack / fungal-type vacuole membrane / vesicle docking involved in exocytosis / endosomal transport / vesicle-mediated transport / protein-membrane adaptor activity / intracellular protein transport / RING-type E3 ubiquitin transferase / autophagy / endocytosis / ubiquitin protein ligase activity / late endosome / actin binding / GTPase binding / early endosome membrane / protein-macromolecule adaptor activity / endosome / zinc ion binding / ATP binding / membrane / cytoplasm / cytosol Similarity search - Function | |||||||||||||||||||||||||||
| Biological species | ![]() | |||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.6 Å | |||||||||||||||||||||||||||
Authors | Shvarev, D. / Ungermann, C. / Moeller, A. | |||||||||||||||||||||||||||
| Funding support | Germany, 6items
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Citation | Journal: Nat Commun / Year: 2024Title: Structure of the endosomal CORVET tethering complex. Authors: Dmitry Shvarev / Caroline König / Nicole Susan / Lars Langemeyer / Stefan Walter / Angela Perz / Florian Fröhlich / Christian Ungermann / Arne Moeller / ![]() Abstract: Cells depend on their endolysosomal system for nutrient uptake and downregulation of plasma membrane proteins. These processes rely on endosomal maturation, which requires multiple membrane fusion ...Cells depend on their endolysosomal system for nutrient uptake and downregulation of plasma membrane proteins. These processes rely on endosomal maturation, which requires multiple membrane fusion steps. Early endosome fusion is promoted by the Rab5 GTPase and its effector, the hexameric CORVET tethering complex, which is homologous to the lysosomal HOPS. How these related complexes recognize their specific target membranes remains entirely elusive. Here, we solve the structure of CORVET by cryo-electron microscopy and revealed its minimal requirements for membrane tethering. As expected, the core of CORVET and HOPS resembles each other. However, the function-defining subunits show marked structural differences. Notably, we discover that unlike HOPS, CORVET depends not only on Rab5 but also on phosphatidylinositol-3-phosphate (PI3P) and membrane lipid packing defects for tethering, implying that an organelle-specific membrane code enables fusion. Our data suggest that both shape and membrane interactions of CORVET and HOPS are conserved in metazoans, thus providing a paradigm how tethering complexes function. | |||||||||||||||||||||||||||
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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 | 8qx8.cif.gz | 753.3 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb8qx8.ent.gz | 562.7 KB | Display | PDB format |
| PDBx/mmJSON format | 8qx8.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 8qx8_validation.pdf.gz | 812.3 KB | Display | wwPDB validaton report |
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| Full document | 8qx8_full_validation.pdf.gz | 851.8 KB | Display | |
| Data in XML | 8qx8_validation.xml.gz | 99.6 KB | Display | |
| Data in CIF | 8qx8_validation.cif.gz | 163.1 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qx/8qx8 ftp://data.pdbj.org/pub/pdb/validation_reports/qx/8qx8 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 18701MC 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
-Vacuolar protein sorting-associated protein ... , 4 types, 4 molecules FDBE
| #1: Protein | Mass: 148102.172 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: VPS8, VPT8, YAL002W, FUN15 / Production host: ![]() |
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| #2: Protein | Mass: 79354.977 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: VPS33, SLP1, VAM5, YLR396C, L8084.15 / Production host: ![]() |
| #3: Protein | Mass: 92857.000 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: VPS16, VAM9, VPT16, YPL045W / Production host: ![]() |
| #5: Protein | Mass: 117069.008 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: VPS3, VPT17, YDR495C, D9719.1 / Production host: ![]() |
-Protein , 2 types, 2 molecules AC
| #4: Protein | Mass: 117617.219 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: PEP5, END1, VAM1, VPL9, VPS11, VPT11, YMR231W, YM9959.13 Production host: ![]() References: UniProt: P12868, RING-type E3 ubiquitin transferase |
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| #6: Protein | Mass: 107531.047 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: PEP3, VAM8, VPS18, VPT18, YLR148W, L9634.2 / Production host: ![]() |
-Details
| Has protein modification | Y |
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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: Endosomal membrane tethering complex CORVET / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT |
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| Source (natural) | Organism: ![]() |
| Source (recombinant) | Organism: ![]() |
| Buffer solution | pH: 7.4 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE |
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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 defocus max: 1800 nm / Nominal defocus min: 800 nm |
| Specimen holder | Cryogen: NITROGEN |
| Image recording | Electron dose: 50 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: 4.6 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 219391 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi






Germany, 6items
Citation







PDBj




FIELD EMISSION GUN