6v69

<StructureSection load='6v69' size='340' side='right'caption='[[6v69]], [[Resolution|resolution]] 4.20&Aring;' scene=''>

<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>

[[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.

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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== References ==

</StructureSection>

[[Category: Chait, B T]]

[[Category: Kapoor, T M]]

[[Category: Molloy, K R]]

[[Category: Ti, S]]

[[Category: Urnavicius, L]]

[[Category: Wieczorek, M]]

[[Category: Structural protein]]