6v6c

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Current revision (14:36, 6 March 2024) (edit) (undo)
 
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<SX load='6v6c' size='340' side='right' viewer='molstar' caption='[[6v6c]], [[Resolution|resolution]] 4.50&Aring;' scene=''>
<SX load='6v6c' size='340' side='right' viewer='molstar' caption='[[6v6c]], [[Resolution|resolution]] 4.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6v6c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6V6C OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6V6C FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6v6c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6V6C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6V6C FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6v6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v6c OCA], [http://pdbe.org/6v6c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6v6c RCSB], [http://www.ebi.ac.uk/pdbsum/6v6c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6v6c ProSAT]</span></td></tr>
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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]] 4.5&#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=6v6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v6c OCA], [https://pdbe.org/6v6c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6v6c RCSB], [https://www.ebi.ac.uk/pdbsum/6v6c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6v6c ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/GCP6_HUMAN GCP6_HUMAN]] Autosomal recessive chorioretinopathy-microcephaly syndrome. The disease is caused by mutations affecting the gene represented in this entry.
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[https://www.uniprot.org/uniprot/GCP6_HUMAN GCP6_HUMAN] Autosomal recessive chorioretinopathy-microcephaly syndrome. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/GCP6_HUMAN GCP6_HUMAN]] Gamma-tubulin complex is necessary for microtubule nucleation at the centrosome.<ref>PMID:11694571</ref>
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[https://www.uniprot.org/uniprot/GCP6_HUMAN GCP6_HUMAN] Gamma-tubulin complex is necessary for microtubule nucleation at the centrosome.<ref>PMID:11694571</ref>
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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 an essential regulator of centrosomal and acentrosomal microtubule formation, yet its structure is not known. Here, we present a cryo-EM reconstruction of the native human gamma-TuRC at approximately 3.8 A resolution, revealing an asymmetric, cone-shaped structure. Pseudo-atomic models indicate that GCP4, GCP5, and GCP6 form distinct Y-shaped assemblies that structurally mimic GCP2/GCP3 subcomplexes distal to the gamma-TuRC "seam." We also identify an unanticipated structural bridge that includes an actin-like protein and spans the gamma-TuRC lumen. Despite its asymmetric architecture, the gamma-TuRC arranges gamma-tubulins into a helical geometry poised to nucleate microtubules. Diversity in the gamma-TuRC subunits introduces large (&gt;100,000 A(2)) surfaces in the complex that allow for interactions with different regulatory factors. The observed compositional complexity of the gamma-TuRC could self-regulate its assembly into a cone-shaped structure to control microtubule formation across diverse contexts, e.g., within biological condensates or alongside existing filaments.
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Asymmetric Molecular Architecture of the Human gamma-Tubulin Ring Complex.,Wieczorek M, Urnavicius L, Ti SC, Molloy KR, Chait BT, Kapoor TM Cell. 2019 Dec 13. pii: S0092-8674(19)31369-8. doi: 10.1016/j.cell.2019.12.007. PMID:31862189<ref>PMID:31862189</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6v6c" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chait, B T]]
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[[Category: Chait BT]]
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[[Category: Kapoor, T M]]
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[[Category: Kapoor TM]]
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[[Category: Molloy, K R]]
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[[Category: Molloy KR]]
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[[Category: Ti, S]]
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[[Category: Ti S]]
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[[Category: Urnavicius, L]]
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[[Category: Urnavicius L]]
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[[Category: Wieczorek, M]]
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[[Category: Wieczorek M]]
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[[Category: G-turc]]
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[[Category: Gamma-tubulin ring complex]]
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[[Category: Gcp]]
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[[Category: Gcp6]]
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[[Category: Gturc]]
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[[Category: Microtubule]]
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[[Category: Microtubule nucleation]]
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[[Category: Single particle cryo-em structure]]
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[[Category: Structural protein]]
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Current revision

Structure of GCP6 in the native human gamma-tubulin ring complex

6v6c, resolution 4.50Å

Proteopedia Page Contributors and Editors (what is this?)

OCA

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