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Open data
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Basic information
| Entry | Database: PDB / ID: 7qpg | ||||||
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| Title | Human RZZ kinetochore corona complex. | ||||||
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Keywords | CELL CYCLE / Kinetochore / centromere / chromosome segregation / mitosis | ||||||
| Function / homology | Function and homology informationprotein localization to kinetochore involved in kinetochore assembly / Dsl1/NZR complex / RZZ complex / regulation of attachment of spindle microtubules to kinetochore / kinetochore microtubule / centromeric DNA binding / regulation of exit from mitosis / protein localization to kinetochore / retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum / COPI-dependent Golgi-to-ER retrograde traffic ...protein localization to kinetochore involved in kinetochore assembly / Dsl1/NZR complex / RZZ complex / regulation of attachment of spindle microtubules to kinetochore / kinetochore microtubule / centromeric DNA binding / regulation of exit from mitosis / protein localization to kinetochore / retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum / COPI-dependent Golgi-to-ER retrograde traffic / mitotic metaphase chromosome alignment / mitotic spindle assembly checkpoint signaling / Golgi organization / establishment of mitotic spindle orientation / mitotic sister chromatid segregation / endoplasmic reticulum to Golgi vesicle-mediated transport / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / lipid droplet / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Resolution of Sister Chromatid Cohesion / bioluminescence / generation of precursor metabolites and energy / meiotic cell cycle / RHO GTPases Activate Formins / kinetochore / small GTPase binding / spindle pole / Separation of Sister Chromatids / protein transport / actin cytoskeleton / protein-containing complex assembly / cell division / endoplasmic reticulum membrane / endoplasmic reticulum / nucleus / membrane / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.9 Å | ||||||
Authors | Raisch, T. / Ciossani, G. / d'Amico, E. / Cmetowski, V. / Carmignani, S. / Maffini, S. / Merino, F. / Wohlgemuth, S. / Vetter, I.R. / Raunser, S. / Musacchio, A. | ||||||
| Funding support | Germany, 1items
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Citation | Journal: EMBO J / Year: 2022Title: Structure of the RZZ complex and molecular basis of Spindly-driven corona assembly at human kinetochores. Authors: Tobias Raisch / Giuseppe Ciossani / Ennio d'Amico / Verena Cmentowski / Sara Carmignani / Stefano Maffini / Felipe Merino / Sabine Wohlgemuth / Ingrid R Vetter / Stefan Raunser / Andrea Musacchio / ![]() Abstract: In metazoans, a ≈1 megadalton (MDa) multiprotein complex comprising the dynein-dynactin adaptor Spindly and the ROD-Zwilch-ZW10 (RZZ) complex is the building block of a fibrous biopolymer, the ...In metazoans, a ≈1 megadalton (MDa) multiprotein complex comprising the dynein-dynactin adaptor Spindly and the ROD-Zwilch-ZW10 (RZZ) complex is the building block of a fibrous biopolymer, the kinetochore fibrous corona. The corona assembles on mitotic kinetochores to promote microtubule capture and spindle assembly checkpoint (SAC) signaling. We report here a high-resolution cryo-EM structure that captures the essential features of the RZZ complex, including a farnesyl-binding site required for Spindly binding. Using a highly predictive in vitro assay, we demonstrate that the SAC kinase MPS1 is necessary and sufficient for corona assembly at supercritical concentrations of the RZZ-Spindly (RZZS) complex, and describe the molecular mechanism of phosphorylation-dependent filament nucleation. We identify several structural requirements for RZZS polymerization in rings and sheets. Finally, we identify determinants of kinetochore localization and corona assembly of Spindly. Our results describe a framework for the long-sought-for molecular basis of corona assembly on metazoan kinetochores. | ||||||
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Structure visualization
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| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 7qpg.cif.gz | 1.2 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb7qpg.ent.gz | 1021.9 KB | Display | PDB format |
| PDBx/mmJSON format | 7qpg.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qp/7qpg ftp://data.pdbj.org/pub/pdb/validation_reports/qp/7qpg | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 14120MC M: map data used to model this data C: citing same article ( |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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Components
| #1: Protein | Mass: 67293.805 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ZWILCH / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q9H900#2: Protein | Mass: 279805.562 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: DS885_16260, KNTC1, KIAA0166 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: A0A366VY15, UniProt: P50748#3: Protein | Mass: 88940.336 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ZW10 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: O43264 |
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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: RZZ complex / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT |
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| Source (natural) | Organism: Homo sapiens (human) |
| Source (recombinant) | Organism: Trichoplusia ni (cabbage looper) |
| Buffer solution | pH: 8 |
| Specimen | Conc.: 5 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TITAN KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: OTHER |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2700 nm / Nominal defocus min: 1200 nm |
| Image recording | Electron dose: 60 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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| 3D reconstruction | Resolution: 3.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 191979 / Symmetry type: POINT |
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About Yorodumi




Homo sapiens (human)
Germany, 1items
Citation
UCSF Chimera





PDBj







Trichoplusia ni (cabbage looper)
