+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-17342 | |||||||||||||||
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Title | Human Commander complex (native) | |||||||||||||||
Map data | ||||||||||||||||
Sample |
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Keywords | COMMD fold / calponin homology fold / pseudo-C5 symmetry / UNKNOWN FUNCTION | |||||||||||||||
Function / homology | Function and homology information negative regulation of sodium ion transmembrane transport / retromer, cargo-selective complex / WNT ligand biogenesis and trafficking / plasma membrane to endosome transport / cytoplasmic sequestering of NF-kappaB / regulation of proteasomal ubiquitin-dependent protein catabolic process / endosome transport via multivesicular body sorting pathway / retromer complex / copper ion homeostasis / negative regulation of protein localization to cell surface ...negative regulation of sodium ion transmembrane transport / retromer, cargo-selective complex / WNT ligand biogenesis and trafficking / plasma membrane to endosome transport / cytoplasmic sequestering of NF-kappaB / regulation of proteasomal ubiquitin-dependent protein catabolic process / endosome transport via multivesicular body sorting pathway / retromer complex / copper ion homeostasis / negative regulation of protein localization to cell surface / Golgi to plasma membrane transport / phosphatidic acid binding / positive regulation of ubiquitin-dependent protein catabolic process / endocytic recycling / phosphatidylinositol-3,4-bisphosphate binding / sodium channel inhibitor activity / retrograde transport, endosome to Golgi / phosphatidylinositol-3,5-bisphosphate binding / Cul2-RING ubiquitin ligase complex / regulation of early endosome to late endosome transport / sodium ion transport / negative regulation of NF-kappaB transcription factor activity / cullin family protein binding / phosphatidylinositol-3,4,5-trisphosphate binding / ficolin-1-rich granule membrane / intracellular copper ion homeostasis / NF-kappaB binding / negative regulation of canonical NF-kappaB signal transduction / tumor necrosis factor-mediated signaling pathway / phosphatidylinositol-4,5-bisphosphate binding / guanyl-nucleotide exchange factor activity / cholesterol homeostasis / positive regulation of protein ubiquitination / nucleotide-excision repair / intracellular protein transport / recycling endosome / small GTPase binding / protein transport / late endosome / Neddylation / cytoplasmic vesicle / positive regulation of canonical NF-kappaB signal transduction / secretory granule lumen / ficolin-1-rich granule lumen / early endosome / endosome membrane / endosome / copper ion binding / intracellular membrane-bounded organelle / centrosome / negative regulation of DNA-templated transcription / Neutrophil degranulation / Golgi apparatus / protein homodimerization activity / extracellular region / nucleoplasm / identical protein binding / metal ion binding / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | |||||||||||||||
Biological species | Homo sapiens (human) | |||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.3 Å | |||||||||||||||
Authors | Kumpula EP / Huiskonen JT | |||||||||||||||
Funding support | Finland, 4 items
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Citation | Journal: Nat Struct Mol Biol / Year: 2024 Title: Structure and interactions of the endogenous human Commander complex. Authors: Saara Laulumaa / Esa-Pekka Kumpula / Juha T Huiskonen / Markku Varjosalo / Abstract: The Commander complex, a 16-protein assembly, plays multiple roles in cell homeostasis, cell cycle and immune response. It consists of copper-metabolism Murr1 domain proteins (COMMD1-10), coiled-coil ...The Commander complex, a 16-protein assembly, plays multiple roles in cell homeostasis, cell cycle and immune response. It consists of copper-metabolism Murr1 domain proteins (COMMD1-10), coiled-coil domain-containing proteins (CCDC22 and CCDC93), DENND10 and the Retriever subcomplex (VPS26C, VPS29 and VPS35L), all expressed ubiquitously in the body and linked to various diseases. Here, we report the structure and key interactions of the endogenous human Commander complex by cryogenic-electron microscopy and mass spectrometry-based proteomics. The complex consists of a stable core of COMMD1-10 and an effector containing DENND10 and Retriever, scaffolded together by CCDC22 and CCDC93. We establish the composition of Commander and reveal major interaction interfaces. These findings clarify its roles in intracellular transport, and uncover a strong association with cilium assembly, and centrosome and centriole functions. | |||||||||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_17342.map.gz | 683.8 MB | EMDB map data format | |
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Header (meta data) | emd-17342-v30.xml emd-17342.xml | 29.5 KB 29.5 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_17342_fsc.xml | 19.2 KB | Display | FSC data file |
Images | emd_17342.png | 80 KB | ||
Masks | emd_17342_msk_1.map | 729 MB | Mask map | |
Filedesc metadata | emd-17342.cif.gz | 8.2 KB | ||
Others | emd_17342_half_map_1.map.gz emd_17342_half_map_2.map.gz | 677.4 MB 677.4 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-17342 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-17342 | HTTPS FTP |
-Related structure data
Related structure data | 8p0vC 8p0wC 8p0xC 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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Related items in Molecule of the Month |
-Map
File | Download / File: emd_17342.map.gz / Format: CCP4 / Size: 729 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.84 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
File | emd_17342_msk_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_17342_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_17342_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
+Entire : Human Commander Complex
+Supramolecule #1: Human Commander Complex
+Macromolecule #1: COMMD1
+Macromolecule #2: COMMD2
+Macromolecule #3: COMMD3
+Macromolecule #4: COMMD4
+Macromolecule #5: COMMD5
+Macromolecule #6: COMMD6
+Macromolecule #7: COMMD7
+Macromolecule #8: COMMD8
+Macromolecule #9: COMMD9
+Macromolecule #10: COMMD10
+Macromolecule #11: CCDC93
+Macromolecule #12: CCDC22
+Macromolecule #13: VPS29
+Macromolecule #14: VPS35L
+Macromolecule #15: VPS26C
+Macromolecule #16: DENND10
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Concentration | 0.1 mg/mL |
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Buffer | pH: 7.4 |
Grid | Model: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 200 / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Support film - Film thickness: 2 / Pretreatment - Type: PLASMA CLEANING / Pretreatment - Time: 50 sec. / Pretreatment - Atmosphere: OTHER / Pretreatment - Pressure: 0.107 kPa |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 279 K / Instrument: FEI VITROBOT MARK IV |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.5 µm / Nominal magnification: 165000 |
Specialist optics | Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV |
Sample stage | Cooling holder cryogen: NITROGEN |
Image recording | Film or detector model: GATAN K2 BASE (4k x 4k) / Number grids imaged: 1 / Number real images: 5884 / Average electron dose: 42.8 e/Å2 |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |