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7QJA

Structure of recombinant human gamma-Tubulin Ring Complex 12-spoked assembly intermediate (spokes 1-12, homogeneous dataset)

This is a non-PDB format compatible entry.
Summary for 7QJA
Entry DOI10.2210/pdb7qja/pdb
EMDB information14015
Descriptoractin, cytoplasmic 1, Gamma-tubulin complex component 5, Gamma-tubulin complex component 3, ... (8 entities in total)
Functional Keywordsassembly, intermediate, complex, cytosolic protein
Biological sourceHomo sapiens (human)
More
Total number of polymer chains37
Total formula weight2738541.19
Authors
Zupa, E.,Pfeffer, S. (deposition date: 2021-12-16, release date: 2022-01-26, Last modification date: 2024-07-17)
Primary citationWurtz, M.,Zupa, E.,Atorino, E.S.,Neuner, A.,Bohler, A.,Rahadian, A.S.,Vermeulen, B.J.A.,Tonon, G.,Eustermann, S.,Schiebel, E.,Pfeffer, S.
Modular assembly of the principal microtubule nucleator gamma-TuRC.
Nat Commun, 13:473-473, 2022
Cited by
PubMed 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, 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.
PubMed: 35078983
DOI: 10.1038/s41467-022-28079-0
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (9.2 Å)
Structure validation

226707

건을2024-10-30부터공개중

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