9smx: Difference between revisions
From Proteopedia
Jump to navigationJump to search
New page: '''Unreleased structure''' The entry 9smx is ON HOLD Authors: Description: Category: Unreleased Structures |
No edit summary |
||
| (One intermediate revision by the same user not shown) | |||
| Line 1: | Line 1: | ||
==CM1-activated gTuRC in complex with nascent alpha-E254D mutant microtubules== | |||
<StructureSection load='9smx' size='340' side='right'caption='[[9smx]], [[Resolution|resolution]] 3.67Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9smx]] is a 57 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9SMX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9SMX FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.67Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene></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=9smx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9smx OCA], [https://pdbe.org/9smx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9smx RCSB], [https://www.ebi.ac.uk/pdbsum/9smx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9smx ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/GCP3_HUMAN GCP3_HUMAN] Gamma-tubulin complex is necessary for microtubule nucleation at the centrosome. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Microtubule nucleation by the gamma-tubulin ring complex (gammaTuRC) is spatiotemporally regulated and in higher eukaryotes is thought to involve a transition from an inactive open to an active closed conformation that matches the microtubule geometry. However, gammaTuRC activators only promote a partially closed conformation, raising the question of whether complete closure is required for activation. Combining in vitro nucleation assays and cryo-EM, we find that centrosomin motif 1 (CM1), a conserved element of several gammaTuRC regulators, potently accelerates human gammaTuRC-mediated microtubule nucleation by facilitating complete closure of gammaTuRC as the nascent microtubule assembles. A 3.7 A cryo-EM structure identifies the gammaTuRC latch and several interactions involved in conformational closure. Notably, the distinct subunits that keep gammaTuRC open and inactive in higher eukaryotes also participate in its closure and activation. This work provides additional insight into the logic of the human gammaTuRC architecture and its activation by CM1. | |||
Structural basis of human gammaTuRC closure during CM1-activated microtubule nucleation.,Serna M, Brito C, Speroni S, Zimmermann F, Lopez-Perrote A, Gili M, Lacasa C, Luders J, Surrey T, Llorca O Nat Commun. 2026 Mar 26. doi: 10.1038/s41467-026-70773-w. PMID:41888131<ref>PMID:41888131</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 9smx" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Saccharomyces cerevisiae S288C]] | |||
[[Category: Llorca O]] | |||
[[Category: Lopez-Perrote A]] | |||
[[Category: Serna M]] | |||
