7m2w
From Proteopedia
(Difference between revisions)
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| - | ==== | + | ==Engineered disulfide cross-linked closed conformation of the Yeast gamma-TuRC(SS)== |
| - | <StructureSection load='7m2w' size='340' side='right'caption='[[7m2w]]' scene=''> | + | <StructureSection load='7m2w' size='340' side='right'caption='[[7m2w]], [[Resolution|resolution]] 3.00Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7m2w]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7M2W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7M2W FirstGlance]. <br> |
| - | </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=7m2w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7m2w OCA], [https://pdbe.org/7m2w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7m2w RCSB], [https://www.ebi.ac.uk/pdbsum/7m2w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7m2w ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene></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=7m2w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7m2w OCA], [https://pdbe.org/7m2w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7m2w RCSB], [https://www.ebi.ac.uk/pdbsum/7m2w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7m2w ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/TBG_YEAST TBG_YEAST] 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, suggesting that it is involved in the minus-end nucleation of microtubule assembly. TUB4 is an important spindle pole body component that organizes both cytoplasmic and nuclear microtubule arrays. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Microtubule (MT) nucleation is regulated by the gamma-tubulin ring complex (gammaTuRC), conserved from yeast to humans. In Saccharomyces cerevisiae, gammaTuRC is composed of seven identical gamma-tubulin small complex (gammaTuSC) sub-assemblies, which associate helically to template MT growth. gammaTuRC assembly provides a key point of regulation for the MT cytoskeleton. Here, we combine crosslinking mass spectrometry, X-ray crystallography, and cryo-EM structures of both monomeric and dimeric gammaTuSCs, and open and closed helical gammaTuRC assemblies in complex with Spc110p to elucidate the mechanisms of gammaTuRC assembly. gammaTuRC assembly is substantially aided by the evolutionarily conserved CM1 motif in Spc110p spanning a pair of adjacent gammaTuSCs. By providing the highest resolution and most complete views of any gammaTuSC assembly, our structures allow phosphorylation sites to be mapped, surprisingly suggesting that they are mostly inhibitory. A comparison of our structures with the CM1 binding site in the human gammaTuRC structure at the interface between GCP2 and GCP6 allows for the interpretation of significant structural changes arising from CM1 helix binding to metazoan gammaTuRC. | ||
| + | |||
| + | CM1-driven assembly and activation of yeast gamma-tubulin small complex underlies microtubule nucleation.,Brilot AF, Lyon AS, Zelter A, Viswanath S, Maxwell A, MacCoss MJ, Muller EG, Sali A, Davis TN, Agard DA Elife. 2021 May 5;10. pii: 65168. doi: 10.7554/eLife.65168. PMID:33949948<ref>PMID:33949948</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7m2w" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Tubulin 3D Structures|Tubulin 3D Structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Saccharomyces cerevisiae S288C]] |
| + | [[Category: Agard DA]] | ||
| + | [[Category: Brilot AF]] | ||
| + | [[Category: Davis TN]] | ||
| + | [[Category: Lyon AS]] | ||
| + | [[Category: MacCoss MJ]] | ||
| + | [[Category: Maxwell A]] | ||
| + | [[Category: Muller EG]] | ||
| + | [[Category: Sali A]] | ||
| + | [[Category: Viswanath S]] | ||
| + | [[Category: Zelter A]] | ||
Current revision
Engineered disulfide cross-linked closed conformation of the Yeast gamma-TuRC(SS)
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