+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-28827 | ||||||||||||||||||||||||||||||
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Title | Human CCC complex | ||||||||||||||||||||||||||||||
Map data | Post-processed sharpened map. B factor -24 | ||||||||||||||||||||||||||||||
Sample |
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Keywords | endosomal sorting / commander / CCC complex / ENDOCYTOSIS | ||||||||||||||||||||||||||||||
Function / homology | Function and homology information negative regulation of sodium ion transmembrane transport / cytoplasmic sequestering of NF-kappaB / plasma membrane to endosome transport / regulation of proteasomal ubiquitin-dependent protein catabolic process / negative regulation of protein localization to cell surface / copper ion homeostasis / Golgi to plasma membrane transport / phosphatidic acid binding / sodium channel inhibitor activity / positive regulation of ubiquitin-dependent protein catabolic process ...negative regulation of sodium ion transmembrane transport / cytoplasmic sequestering of NF-kappaB / plasma membrane to endosome transport / regulation of proteasomal ubiquitin-dependent protein catabolic process / negative regulation of protein localization to cell surface / copper ion homeostasis / Golgi to plasma membrane transport / phosphatidic acid binding / sodium channel inhibitor activity / positive regulation of ubiquitin-dependent protein catabolic process / phosphatidylinositol-3,4-bisphosphate binding / endocytic recycling / phosphatidylinositol-3,5-bisphosphate binding / Cul2-RING ubiquitin ligase complex / negative regulation of NF-kappaB transcription factor activity / sodium ion transport / phosphatidylinositol-3,4,5-trisphosphate binding / cullin family protein binding / NF-kappaB binding / intracellular copper ion homeostasis / negative regulation of canonical NF-kappaB signal transduction / phosphatidylinositol-4,5-bisphosphate binding / tumor necrosis factor-mediated signaling pathway / cholesterol homeostasis / positive regulation of protein ubiquitination / nucleotide-excision repair / recycling endosome / protein transport / Neddylation / cytoplasmic vesicle / secretory granule lumen / positive regulation of canonical NF-kappaB signal transduction / ficolin-1-rich granule lumen / early endosome / endosome membrane / endosome / copper ion binding / intracellular membrane-bounded organelle / negative regulation of DNA-templated transcription / centrosome / Neutrophil degranulation / Golgi apparatus / protein homodimerization activity / extracellular region / nucleoplasm / identical protein binding / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||||||||||||||||||||||||||
Biological species | Homo sapiens (human) | ||||||||||||||||||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.53 Å | ||||||||||||||||||||||||||||||
Authors | Healy MD / McNally KE / Butkovic R / Chilton M / Kato K / Sacharz J / McConville C / Moody ERR / Shaw S / Planelles-Herrero VJ ...Healy MD / McNally KE / Butkovic R / Chilton M / Kato K / Sacharz J / McConville C / Moody ERR / Shaw S / Planelles-Herrero VJ / Kadapalakere SY / Ross J / Borucu U / Palmer CS / Chen K / Croll TI / Hall RJ / Caruana NJ / Ghai R / Nguyen THD / Heesom KJ / Saitoh S / Berger I / Berger-Schaffitzel C / Williams TA / Stroud DA / Derivery E / Collins BM / Cullen PJ | ||||||||||||||||||||||||||||||
Funding support | United Kingdom, Australia, 9 items
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Citation | Journal: Cell / Year: 2023 Title: Structure of the endosomal Commander complex linked to Ritscher-Schinzel syndrome. Authors: Michael D Healy / Kerrie E McNally / Rebeka Butkovič / Molly Chilton / Kohji Kato / Joanna Sacharz / Calum McConville / Edmund R R Moody / Shrestha Shaw / Vicente J Planelles-Herrero / ...Authors: Michael D Healy / Kerrie E McNally / Rebeka Butkovič / Molly Chilton / Kohji Kato / Joanna Sacharz / Calum McConville / Edmund R R Moody / Shrestha Shaw / Vicente J Planelles-Herrero / Sathish K N Yadav / Jennifer Ross / Ufuk Borucu / Catherine S Palmer / Kai-En Chen / Tristan I Croll / Ryan J Hall / Nikeisha J Caruana / Rajesh Ghai / Thi H D Nguyen / Kate J Heesom / Shinji Saitoh / Imre Berger / Christiane Schaffitzel / Tom A Williams / David A Stroud / Emmanuel Derivery / Brett M Collins / Peter J Cullen / Abstract: The Commander complex is required for endosomal recycling of diverse transmembrane cargos and is mutated in Ritscher-Schinzel syndrome. It comprises two sub-assemblies: Retriever composed of VPS35L, ...The Commander complex is required for endosomal recycling of diverse transmembrane cargos and is mutated in Ritscher-Schinzel syndrome. It comprises two sub-assemblies: Retriever composed of VPS35L, VPS26C, and VPS29; and the CCC complex which contains twelve subunits: COMMD1-COMMD10 and the coiled-coil domain-containing (CCDC) proteins CCDC22 and CCDC93. Combining X-ray crystallography, electron cryomicroscopy, and in silico predictions, we have assembled a complete structural model of Commander. Retriever is distantly related to the endosomal Retromer complex but has unique features preventing the shared VPS29 subunit from interacting with Retromer-associated factors. The COMMD proteins form a distinctive hetero-decameric ring stabilized by extensive interactions with CCDC22 and CCDC93. These adopt a coiled-coil structure that connects the CCC and Retriever assemblies and recruits a 16th subunit, DENND10, to form the complete Commander complex. The structure allows mapping of disease-causing mutations and reveals the molecular features required for the function of this evolutionarily conserved trafficking machinery. | ||||||||||||||||||||||||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_28827.map.gz | 64.8 MB | EMDB map data format | |
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Header (meta data) | emd-28827-v30.xml emd-28827.xml | 35.4 KB 35.4 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_28827_fsc.xml | 9.4 KB | Display | FSC data file |
Images | emd_28827.png | 53.3 KB | ||
Filedesc metadata | emd-28827.cif.gz | 8.7 KB | ||
Others | emd_28827_additional_1.map.gz emd_28827_half_map_1.map.gz emd_28827_half_map_2.map.gz | 54.7 MB 54.9 MB 54.9 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-28827 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-28827 | HTTPS FTP |
-Validation report
Summary document | emd_28827_validation.pdf.gz | 1.2 MB | Display | EMDB validaton report |
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Full document | emd_28827_full_validation.pdf.gz | 1.2 MB | Display | |
Data in XML | emd_28827_validation.xml.gz | 16.3 KB | Display | |
Data in CIF | emd_28827_validation.cif.gz | 21.3 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-28827 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-28827 | HTTPS FTP |
-Related structure data
Related structure data | 8f2uMC 8esdC 8eseC 8f2rC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_28827.map.gz / Format: CCP4 / Size: 70.2 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Annotation | Post-processed sharpened map. B factor -24 | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.084 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Additional map: Refine 3D map
File | emd_28827_additional_1.map | ||||||||||||
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Annotation | Refine 3D map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half map
File | emd_28827_half_map_1.map | ||||||||||||
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Annotation | Half map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half map
File | emd_28827_half_map_2.map | ||||||||||||
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Annotation | Half map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
+Entire : Human CCC complex
+Supramolecule #1: Human CCC complex
+Macromolecule #1: COMM domain-containing protein 1
+Macromolecule #2: COMM domain-containing protein 2
+Macromolecule #3: COMM domain-containing protein 3
+Macromolecule #4: COMM domain-containing protein 4
+Macromolecule #5: COMM domain-containing protein 5
+Macromolecule #6: COMM domain-containing protein 6
+Macromolecule #7: COMM domain-containing protein 7
+Macromolecule #8: COMM domain-containing protein 8
+Macromolecule #9: COMM domain-containing protein 9
+Macromolecule #10: COMM domain-containing protein 10
+Macromolecule #11: Coiled-coil domain-containing protein 93
+Macromolecule #12: Coiled-coil domain-containing protein 22
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Concentration | 0.2 mg/mL |
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Buffer | pH: 7.2 Details: 50 mM HEPES pH7.2, 150 mM NaCl, 2mM beta-mercaptoethanol, 0.01% Triton-X100 |
Grid | Model: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300 / Support film - Material: GRAPHENE OXIDE |
Vitrification | Cryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV |
Details | Human CCC complex cross-linked with 1 mM BS3 |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Number grids imaged: 2 / Number real images: 5651 / Average exposure time: 9.01 sec. / Average electron dose: 43.14 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: 1.2 µm |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |