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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 | |||||||||||||||||||||
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![]() | ENDOCYTOSIS / CORVET / membrane fusion / endosome / Rab GTPase / tethering | |||||||||||||||||||||
Function / homology | ![]() histone catabolic process / organelle fusion / CORVET complex / regulation of SNARE complex assembly / HOPS complex / endosomal vesicle fusion / vesicle tethering / regulation of vacuole fusion, non-autophagic / vacuole fusion, non-autophagic / Golgi to vacuole transport ...histone catabolic process / organelle fusion / CORVET complex / regulation of SNARE complex assembly / HOPS complex / endosomal vesicle fusion / vesicle tethering / regulation of vacuole fusion, non-autophagic / vacuole fusion, non-autophagic / Golgi to vacuole transport / vacuole inheritance / Golgi to endosome transport / vesicle fusion with vacuole / vesicle docking / late endosome to vacuole transport via multivesicular body sorting pathway / endosome organization / vacuole organization / protein targeting to vacuole / Golgi stack / late endosome to vacuole transport / fungal-type vacuole / piecemeal microautophagy of the nucleus / vacuolar acidification / fungal-type vacuole membrane / vesicle docking involved in exocytosis / endosomal transport / protein-membrane adaptor activity / vesicle-mediated transport / 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 / ATP binding / membrane / metal ion binding / cytosol / cytoplasm Similarity search - Function | |||||||||||||||||||||
Biological species | ![]() ![]() | |||||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.6 Å | |||||||||||||||||||||
![]() | Shvarev, D. / Ungermann, C. / Moeller, A. | |||||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: 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. | |||||||||||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 753.1 KB | Display | ![]() |
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PDB format | ![]() | 562.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 811.7 KB | Display | ![]() |
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Full document | ![]() | 847.9 KB | Display | |
Data in XML | ![]() | 100.7 KB | Display | |
Data in CIF | ![]() | 162 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 18701MC ![]() 7zu0C M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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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: ![]() |
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
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
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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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