8vrd: Difference between revisions
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==Rigid body fitted model for free recombinant gamma tubulin ring complex.== | |||
<StructureSection load='8vrd' size='340' side='right'caption='[[8vrd]], [[Resolution|resolution]] 7.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8vrd]] is a 34 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8VRD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8VRD FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 7Å</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=8vrd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8vrd OCA], [https://pdbe.org/8vrd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8vrd RCSB], [https://www.ebi.ac.uk/pdbsum/8vrd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8vrd ProSAT]</span></td></tr> | |||
</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> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8vrd" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Aher A]] | |||
[[Category: Kapoor TM]] | |||
[[Category: Urnavicius L]] | |||
Latest revision as of 13:03, 9 October 2024
Rigid body fitted model for free recombinant gamma tubulin ring complex.Rigid body fitted model for free recombinant gamma tubulin ring complex.
Structural highlights
Publication Abstract from PubMedMicrotubules 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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