8va2

Symmetry expanded map of 2 gamma-tubulins bound to 2 alpha tubulins in gamma tubulin ring complex capped microtubule end.

spinqualitylabelsall models 8va2, resolution 4.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8va2 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 4.5Å Ligands: GDP, GTP, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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. , PMID:38609661 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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