8qry: Difference between revisions

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'''Unreleased structure'''


The entry 8qry is ON HOLD
==Crystal structure of the yeast spindle body component Spc98==
<StructureSection load='8qry' size='340' side='right'caption='[[8qry]], [[Resolution|resolution]] 1.87&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8qry]] is a 1 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=8QRY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8QRY FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.87&#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=8qry FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8qry OCA], [https://pdbe.org/8qry PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8qry RCSB], [https://www.ebi.ac.uk/pdbsum/8qry PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8qry ProSAT]</span></td></tr>
</table>
<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.


Authors: Bellini, D., Yatskevich, S., Barford, D.
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>


Description: Crystal structure of the yeast spindle body component Spc98
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Bellini, D]]
<div class="pdbe-citations 8qry" style="background-color:#fffaf0;"></div>
[[Category: Barford, D]]
== References ==
[[Category: Yatskevich, S]]
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Barford D]]
[[Category: Bellini D]]
[[Category: Yatskevich S]]
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