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- PDB-7qj8: Structure of recombinant human gamma-Tubulin Ring Complex 12-spok... -
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Open data
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Basic information
Entry | Database: PDB / ID: 7qj8 | |||||||||
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Title | Structure of recombinant human gamma-Tubulin Ring Complex 12-spoked assembly intermediate (spokes 3-14, substoichiometric spokes 1-2) | |||||||||
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![]() | CYTOSOLIC PROTEIN / Assembly / Intermediate / Complex | |||||||||
Function / homology | ![]() microtubule nucleation by interphase microtubule organizing center / gamma-tubulin complex localization / equatorial microtubule organizing center / mitotic spindle microtubule / gamma-tubulin ring complex / interphase microtubule organizing center / polar microtubule / gamma-tubulin complex / meiotic spindle organization / microtubule nucleation ...microtubule nucleation by interphase microtubule organizing center / gamma-tubulin complex localization / equatorial microtubule organizing center / mitotic spindle microtubule / gamma-tubulin ring complex / interphase microtubule organizing center / polar microtubule / gamma-tubulin complex / meiotic spindle organization / microtubule nucleation / gamma-tubulin binding / non-motile cilium / microtubule organizing center / pericentriolar material / cytoplasmic microtubule / cell leading edge / mitotic sister chromatid segregation / mitotic spindle assembly / single fertilization / spindle assembly / cytoplasmic microtubule organization / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / Recruitment of mitotic centrosome proteins and complexes / Recruitment of NuMA to mitotic centrosomes / Anchoring of the basal body to the plasma membrane / centriole / AURKA Activation by TPX2 / mitotic spindle organization / ciliary basal body / condensed nuclear chromosome / meiotic cell cycle / neuron migration / brain development / recycling endosome / structural constituent of cytoskeleton / spindle pole / microtubule cytoskeleton organization / spindle / microtubule cytoskeleton / Regulation of PLK1 Activity at G2/M Transition / apical part of cell / mitotic cell cycle / microtubule binding / protein-containing complex assembly / microtubule / neuron projection / centrosome / GTP binding / structural molecule activity / nucleoplasm / identical protein binding / membrane / nucleus / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 8.7 Å | |||||||||
![]() | Zupa, E. / Pfeffer, S. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Modular assembly of the principal microtubule nucleator γ-TuRC. Authors: Martin Würtz / Erik Zupa / Enrico S Atorino / Annett Neuner / Anna Böhler / Ariani S Rahadian / Bram J A Vermeulen / Giulia Tonon / Sebastian Eustermann / Elmar Schiebel / Stefan Pfeffer / ![]() Abstract: The gamma-tubulin ring complex (γ-TuRC) is the principal microtubule nucleation template in vertebrates. Recent cryo-EM reconstructions visualized the intricate quaternary structure of the γ-TuRC, ...The gamma-tubulin ring complex (γ-TuRC) is the principal microtubule nucleation template in vertebrates. Recent cryo-EM reconstructions visualized the intricate quaternary structure of the γ-TuRC, containing more than thirty subunits, raising fundamental questions about γ-TuRC assembly and the role of actin as an integral part of the complex. Here, we reveal the structural mechanism underlying modular γ-TuRC assembly and identify a functional role of actin in microtubule nucleation. During γ-TuRC assembly, a GCP6-stabilized core comprising GCP2-3-4-5-4-6 is expanded by stepwise recruitment, selective stabilization and conformational locking of four pre-formed GCP2-GCP3 units. Formation of the lumenal bridge specifies incorporation of the terminal GCP2-GCP3 unit and thereby leads to closure of the γ-TuRC ring in a left-handed spiral configuration. Actin incorporation into the complex is not relevant for γ-TuRC assembly and structural integrity, but determines γ-TuRC geometry and is required for efficient microtubule nucleation and mitotic chromosome alignment in vivo. | |||||||||
History |
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Structure visualization
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Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 2.4 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 14013MC ![]() 7qj0C ![]() 7qj1C ![]() 7qj2C ![]() 7qj3C ![]() 7qj4C ![]() 7qj5C ![]() 7qj6C ![]() 7qj7C ![]() 7qj9C ![]() 7qjaC ![]() 7qjbC ![]() 7qjcC ![]() 7qjdC ![]() 7qjeC 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
-Gamma-tubulin complex component ... , 5 types, 17 molecules lJaDFHNhjCEGMIKLc
#1: Protein | Mass: 118467.547 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() References: UniProt: Q96RT8 #5: Protein | Mass: 103710.102 Da / Num. of mol.: 7 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() References: UniProt: Q96CW5 #6: Protein | Mass: 102666.953 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() References: UniProt: Q9BSJ2 #7: Protein | Mass: 76179.969 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() References: UniProt: Q9UGJ1 #8: Protein | Mass: 200733.641 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() References: UniProt: Q96RT7 |
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-Protein , 3 types, 18 molecules 12QRSTUVWXYZebikmd
#2: Protein | Mass: 51227.770 Da / Num. of mol.: 12 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() References: UniProt: P23258 #3: Protein | | Mass: 41782.660 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() References: UniProt: A0A6I9HGD1 #4: Protein | Mass: 8485.724 Da / Num. of mol.: 5 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() References: UniProt: Q08AG7 |
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-Non-polymers , 1 types, 6 molecules ![](data/chem/img/HOH.gif)
#9: Water | ChemComp-HOH / |
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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: Recombinant human Gamma-Tubulin Ring Complex / Type: COMPLEX / Entity ID: #1-#8 / Source: RECOMBINANT |
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Molecular weight | Value: 2.0 MDa / Experimental value: NO |
Source (natural) | Organism: ![]() |
Source (recombinant) | Organism: ![]() |
Buffer solution | pH: 7.5 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Specimen support | Grid material: COPPER / Grid mesh size: 200 divisions/in. / Grid type: Quantifoil R2/1 |
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: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2500 nm / Nominal defocus min: 2000 nm / Cs: 2.7 mm |
Image recording | Electron dose: 35 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) / Num. of grids imaged: 1 / Num. of real images: 6127 |
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Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||||||||||||||||
Particle selection | Num. of particles selected: 436887 | ||||||||||||||||||||||||||||||||||||||||||||||||||
3D reconstruction | Resolution: 8.7 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 5443 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||||||||||||||||||||
Atomic model building | Protocol: FLEXIBLE FIT / Space: REAL | ||||||||||||||||||||||||||||||||||||||||||||||||||
Atomic model building | 3D fitting-ID: 1 / Source name: PDB / Type: experimental model
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