6v6b: Difference between revisions

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'''Unreleased structure'''


The entry 6v6b is ON HOLD  until Paper Publication
==Structures of GCP2 and GCP3 in the native human gamma-tubulin ring complex==
<StructureSection load='6v6b' size='340' side='right'caption='[[6v6b]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6v6b]] 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=6V6B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6V6B 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=6v6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v6b OCA], [http://pdbe.org/6v6b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6v6b RCSB], [http://www.ebi.ac.uk/pdbsum/6v6b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6v6b ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/GCP3_HUMAN GCP3_HUMAN]] Gamma-tubulin complex is necessary for microtubule nucleation at the centrosome. [[http://www.uniprot.org/uniprot/GCP2_HUMAN GCP2_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 6v6b" 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: Gamma-tusc]]
[[Category: Gcp]]
[[Category: Gcp2]]
[[Category: Gcp3]]
[[Category: Gturc]]
[[Category: Gtusc]]
[[Category: Microtubule]]
[[Category: Microtubule nucleation]]
[[Category: Single particle cryo-em structure]]
[[Category: Structural protein]]

Revision as of 11:31, 1 January 2020

Structures of GCP2 and GCP3 in the native human gamma-tubulin ring complexStructures of GCP2 and GCP3 in the native human gamma-tubulin ring complex

Structural highlights

6v6b is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GCP3_HUMAN] Gamma-tubulin complex is necessary for microtubule nucleation at the centrosome. [GCP2_HUMAN] Gamma-tubulin complex is necessary for microtubule nucleation at the centrosome.

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 (>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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Wieczorek M, Urnavicius L, Ti SC, Molloy KR, Chait BT, Kapoor TM. Asymmetric Molecular Architecture of the Human gamma-Tubulin Ring Complex. Cell. 2019 Dec 13. pii: S0092-8674(19)31369-8. doi: 10.1016/j.cell.2019.12.007. PMID:31862189 doi:http://dx.doi.org/10.1016/j.cell.2019.12.007

6v6b, resolution 3.80Å

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OCA