9h9q

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Current revision (06:25, 15 January 2025) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 9h9q is ON HOLD until Paper Publication
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==Candida albicans gamma-tubulin small complex within ring-like higher oligomer in complex with Spc72 CM1==
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<StructureSection load='9h9q' size='340' side='right'caption='[[9h9q]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9h9q]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_albicans Candida albicans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9H9Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9H9Q FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.6&#8491;</td></tr>
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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=9h9q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9h9q OCA], [https://pdbe.org/9h9q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9h9q RCSB], [https://www.ebi.ac.uk/pdbsum/9h9q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9h9q ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A0A8H6F519_CANAX A0A8H6F519_CANAX] Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome.[RuleBase:RU000352]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The gamma-tubulin ring complex (gamma-TuRC) is a structural template for controlled nucleation of microtubules from alpha/beta-tubulin heterodimers. At the cytoplasmic side of the yeast spindle pole body, the CM1-containing receptor protein Spc72 promotes gamma-TuRC assembly from seven gamma-tubulin small complexes (gamma-TuSCs) and recruits the microtubule polymerase Stu2, yet their molecular interplay remains unclear. Here, we determine the cryo-EM structure of the Candida albicans cytoplasmic nucleation unit at 3.6 A resolution, revealing how the gamma-TuRC is assembled and conformationally primed for microtubule nucleation by the dimerised Spc72 CM1 motif. Two coiled-coil regions of Spc72 interact with the conserved C-terminal alpha-helix of Stu2 and thereby position the alpha/beta-tubulin-binding TOG domains of Stu2 in the vicinity of the microtubule assembly site. Collectively, we reveal the function of CM1 motifs in gamma-TuSC oligomerisation and the recruitment of microtubule polymerases to the gamma-TuRC.
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Authors:
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Structural insights into the interplay between microtubule polymerases, gamma-tubulin complexes and their receptors.,Zheng A, Vermeulen BJA, Wurtz M, Neuner A, Lubbehusen N, Mayer MP, Schiebel E, Pfeffer S Nat Commun. 2025 Jan 5;16(1):402. doi: 10.1038/s41467-024-55778-7. PMID:39757296<ref>PMID:39757296</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 9h9q" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Candida albicans]]
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[[Category: Large Structures]]
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[[Category: Pfeffer S]]
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[[Category: Vermeulen BJA]]

Current revision

Candida albicans gamma-tubulin small complex within ring-like higher oligomer in complex with Spc72 CM1

PDB ID 9h9q

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