8va2: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8va2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8va2 OCA], [https://pdbe.org/8va2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8va2 RCSB], [https://www.ebi.ac.uk/pdbsum/8va2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8va2 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8va2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8va2 OCA], [https://pdbe.org/8va2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8va2 RCSB], [https://www.ebi.ac.uk/pdbsum/8va2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8va2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== | <div style="background-color:#fffaf0;"> | ||
== 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<ref>PMID:38609661</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 8va2" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 10:02, 9 October 2024
Symmetry expanded map of 2 gamma-tubulins bound to 2 alpha tubulins in gamma tubulin ring complex capped microtubule end.
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