8vt7 | pdb_00008vt7

Structure of the gamma tubulin ring complex nucleated microtubule protofilament.

spinqualitylabelsall models 8vt7, resolution 2.66Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8vt7 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.66Å Ligands: GDP, GTP, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease TBB3_HUMAN Congenital fibrosis of extraocular muscles;Cortical dysgenesis with pontocerebellar hypoplasia due to TUBB3 mutation. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. Function TBB3_HUMAN Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. TUBB3 plays a critical role in proper axon guidance and mantainance. Publication Abstract from PubMed Microtubules are composed of alpha-tubulin and beta-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 alpha/beta-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 gamma-tubulin ring complex (gamma-TuRC), an essential regulator of microtubule formation that contains 14 gamma-tubulins, selectively nucleates 13-protofilament microtubules. Cryogenic electron microscopy reconstructions of gamma-TuRC-capped microtubule minus ends reveal the extensive intra-domain and inter-domain motions of gamma-TuRC subunits that accommodate luminal bridge components and establish lateral and longitudinal interactions between gamma-tubulins and alpha-tubulins. Our structures suggest that gamma-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. Structure of the gamma-tubulin ring complex-capped microtubule.,Aher A, Urnavicius L, Xue A, Neselu K, Kapoor TM Nat Struct Mol Biol. 2024 Jul;31(7):1124-1133. doi: 10.1038/s41594-024-01264-z. , Epub 2024 Apr 12. PMID:38609661 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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