View source for 8qv0


==Structure of the native microtubule lattice nucleated from the yeast spindle pole body==
<StructureSection load='8qv0' size='340' side='right'caption='[[8qv0]], [[Resolution|resolution]] 6.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8qv0]] is a 26 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8QV0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8QV0 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]] 6.6&#8491;</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=8qv0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8qv0 OCA], [https://pdbe.org/8qv0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8qv0 RCSB], [https://www.ebi.ac.uk/pdbsum/8qv0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8qv0 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TBA1_YEAST TBA1_YEAST] 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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Microtubule (MT) filaments, composed of alpha/beta-tubulin dimers, are fundamental to cellular architecture, function and organismal development. They are nucleated from MT organizing centers by the evolutionarily conserved gamma-tubulin ring complex (gammaTuRC). However, the molecular mechanism of nucleation remains elusive. Here we used cryo-electron tomography to determine the structure of the native gammaTuRC capping the minus end of a MT in the context of enriched budding yeast spindles. In our structure, gammaTuRC presents a ring of gamma-tubulin subunits to seed nucleation of exclusively 13-protofilament MTs, adopting an active closed conformation to function as a perfect geometric template for MT nucleation. Our cryo-electron tomography reconstruction revealed that a coiled-coil protein staples the first row of alpha/beta-tubulin of the MT to alternating positions along the gamma-tubulin ring of gammaTuRC. This positioning of alpha/beta-tubulin onto gammaTuRC suggests a role for the coiled-coil protein in augmenting gammaTuRC-mediated MT nucleation. Based on our results, we describe a molecular model for budding yeast gammaTuRC activation and MT nucleation.

Structure of the native gamma-tubulin ring complex capping spindle microtubules.,Dendooven T, Yatskevich S, Burt A, Chen ZA, Bellini D, Rappsilber J, Kilmartin JV, Barford D Nat Struct Mol Biol. 2024 Jul;31(7):1134-1144. doi: 10.1038/s41594-024-01281-y. , Epub 2024 Apr 12. PMID:38609662<ref>PMID:38609662</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8qv0" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Barford D]]
[[Category: Bellini D]]
[[Category: Burt A]]
[[Category: Dendooven T]]
[[Category: Kilmartin J]]
[[Category: Yatskevich S]]