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| | ==Structure of the vertebrate gamma-Tubulin Ring Complex== | | ==Structure of the vertebrate gamma-Tubulin Ring Complex== |
| - | <StructureSection load='6tf9' size='340' side='right'caption='[[6tf9]], [[Resolution|resolution]] 4.80Å' scene=''> | + | <SX load='6tf9' size='340' side='right' viewer='molstar' caption='[[6tf9]], [[Resolution|resolution]] 4.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6tf9]] is a 48 chain structure with sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TF9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6TF9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6tf9]] is a 23 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TF9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TF9 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6tf9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tf9 OCA], [http://pdbe.org/6tf9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tf9 RCSB], [http://www.ebi.ac.uk/pdbsum/6tf9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tf9 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]] 4.8Å</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=6tf9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tf9 OCA], [https://pdbe.org/6tf9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tf9 RCSB], [https://www.ebi.ac.uk/pdbsum/6tf9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tf9 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ACTB_XENLA ACTB_XENLA]] Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells. Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction. In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA.[UniProtKB:P60709] [[http://www.uniprot.org/uniprot/TBG1_XENLA TBG1_XENLA]] 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. [[http://www.uniprot.org/uniprot/A0A1L8HGZ5_XENLA A0A1L8HGZ5_XENLA]] Gamma-tubulin complex is necessary for microtubule nucleation at the centrosome.[RuleBase:RU363050] [[http://www.uniprot.org/uniprot/Q642S3_XENLA Q642S3_XENLA]] Gamma-tubulin complex is necessary for microtubule nucleation at the centrosome.[RuleBase:RU363050] | + | [https://www.uniprot.org/uniprot/GCP3_XENLA GCP3_XENLA] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6tf9" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6tf9" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Tubulin 3D Structures|Tubulin 3D Structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| - | </StructureSection> | + | </SX> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Xenopus laevis]] | | [[Category: Xenopus laevis]] |
| - | [[Category: Pfeffer, S]] | + | [[Category: Pfeffer S]] |
| - | [[Category: Zupa, E]] | + | [[Category: Zupa E]] |
| - | [[Category: Cell cycle]]
| + | |
| - | [[Category: Gamma-tubulin ring complex]]
| + | |
| - | [[Category: Microtubule nucleation]]
| + | |
| Structural highlights
Function
GCP3_XENLA
Publication Abstract from PubMed
Microtubules (MTs) are dynamic polymers of alphabeta-tubulin and play critical roles in cell signaling, cell migration, intracellular transport processes and chromosome segregation(1). They assemble de novo from alpha/beta-tubulin dimers in an essential process termed MT nucleation. Complexes containing the protein gamma-tubulin serve as structural templates for the MT nucleation reaction(2). In vertebrates, MTs are nucleated by the 2.2 MDa gamma-tubulin ring complex (gamma-TuRC) composed of gamma-tubulin, five related gamma-tubulin complex proteins (GCP2-6) and additional factors(3). GCP6 is unique among the GCP proteins, because it carries an extended insertion domain of unknown function. High-resolution structural information on the gamma-TuRC is not available, strongly limiting our understanding of MT formation in cells and tissue(2). Here, we present the cryo-EM structure of gamma-TuRC from Xenopus laevis at 4.8 A global resolution, revealing a 14-spoked arrangement of GCPs and gamma-tubulins in a partially flexible open left-handed spiral with a uniform sequence of GCP variants (Fig. 1a). Via specific interactions with other GCP proteins, the GCP6-specific insertion domain scaffolds the assembly of the gamma-TuRC. Unexpectedly, we identified Actin as a bona fide structural component of gamma-TuRC with functional relevance in MT nucleation. The gamma-TuRC spiral geometry is suboptimal for MT nucleation and a controlled conformational rearrangement of the gamma-TuRC is required for its activation. Collectively, our cryo-EM reconstruction provides unprecedented insights into the molecular organization, the assembly and the activation mechanism of vertebrate gamma-TuRC and will serve as an important framework for the mechanistic understanding of fundamental biological processes associated with MT nucleation, e.g. meiotic and mitotic spindle formation and centriole biogensis(4).
Insights into the assembly and activation of the microtubule nucleator gamma-TuRC.,Liu P, Zupa E, Neuner A, Bohler A, Loerke J, Flemming D, Ruppert T, Rudack T, Peter C, Spahn C, Gruss OJ, Pfeffer S, Schiebel E Nature. 2019 Dec 19. pii: 10.1038/s41586-019-1896-6. doi:, 10.1038/s41586-019-1896-6. PMID:31856152[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Liu P, Zupa E, Neuner A, Bohler A, Loerke J, Flemming D, Ruppert T, Rudack T, Peter C, Spahn C, Gruss OJ, Pfeffer S, Schiebel E. Insights into the assembly and activation of the microtubule nucleator gamma-TuRC. Nature. 2019 Dec 19. pii: 10.1038/s41586-019-1896-6. doi:, 10.1038/s41586-019-1896-6. PMID:31856152 doi:http://dx.doi.org/10.1038/s41586-019-1896-6
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