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8VRD

Rigid body fitted model for free recombinant gamma tubulin ring complex.

Summary for 8VRD
Entry DOI10.2210/pdb8vrd/pdb
EMDB information43481
DescriptorGamma-tubulin complex component 3, TUBGCP6 protein, Mitotic-spindle organizing protein 1, ... (8 entities in total)
Functional Keywordscomplex, cytosolic protein
Biological sourceHomo sapiens (human)
More
Total number of polymer chains34
Total formula weight2807021.61
Authors
Aher, A.,Urnavicius, L.,Kapoor, T.M. (deposition date: 2024-01-21, release date: 2024-03-27, Last modification date: 2024-10-09)
Primary citationAher, A.,Urnavicius, L.,Xue, A.,Neselu, K.,Kapoor, T.M.
Structure of the gamma-tubulin ring complex-capped microtubule.
Nat.Struct.Mol.Biol., 31:1124-1133, 2024
Cited by
PubMed Abstract: Microtubules are composed of α-tubulin and β-tubulin dimers positioned head-to-tail to form protofilaments that associate laterally in varying numbers. It is not known how cellular microtubules assemble with the canonical 13-protofilament architecture, resulting in micrometer-scale α/β-tubulin tracks for intracellular transport that align with, rather than spiral along, the long axis of the filament. We report that the human ~2.3 MDa γ-tubulin ring complex (γ-TuRC), an essential regulator of microtubule formation that contains 14 γ-tubulins, selectively nucleates 13-protofilament microtubules. Cryogenic electron microscopy reconstructions of γ-TuRC-capped microtubule minus ends reveal the extensive intra-domain and inter-domain motions of γ-TuRC subunits that accommodate luminal bridge components and establish lateral and longitudinal interactions between γ-tubulins and α-tubulins. Our structures suggest that γ-TuRC, an inefficient nucleation template owing to its splayed conformation, can transform into a compacted cap at the microtubule minus end and set the lattice architecture of cellular microtubules.
PubMed: 38609661
DOI: 10.1038/s41594-024-01264-z
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (7 Å)
Structure validation

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