6v69: Difference between revisions

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'''Unreleased structure'''


The entry 6v69 is ON HOLD  until Paper Publication
==Structures of GCP4 and GCP5 in the native human gamma-tubulin ring complex==
<StructureSection load='6v69' size='340' side='right'caption='[[6v69]], [[Resolution|resolution]] 4.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6v69]] is a 2 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=6V69 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6V69 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=6v69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v69 OCA], [http://pdbe.org/6v69 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6v69 RCSB], [http://www.ebi.ac.uk/pdbsum/6v69 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6v69 ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/GCP5_HUMAN GCP5_HUMAN]] Gamma-tubulin complex is necessary for microtubule nucleation at the centrosome. [[http://www.uniprot.org/uniprot/GCP4_HUMAN GCP4_HUMAN]] Gamma-tubulin complex is necessary for microtubule nucleation at the centrosome.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


Authors:  
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>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 6v69" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Chait, B T]]
[[Category: Kapoor, T M]]
[[Category: Molloy, K R]]
[[Category: Ti, S]]
[[Category: Urnavicius, L]]
[[Category: Wieczorek, M]]
[[Category: G-turc]]
[[Category: Gamma-tubulin ring complex]]
[[Category: Gcp]]
[[Category: Gcp4]]
[[Category: Gcp5]]
[[Category: Gturc]]
[[Category: Microtubule]]
[[Category: Microtubule nucleation]]
[[Category: Single particle cryo-em structure]]
[[Category: Structural protein]]