3q0x: Difference between revisions
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New page: '''Unreleased structure''' The entry 3q0x is ON HOLD Authors: Kitagawa, D., Vakonakis, I., Olieric, N., Hilbert, M., Keller, D., Olieric, V., Bortfeld, M., Erat, M.C., Flueckiger, I., G... |
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The | ==N-terminal coiled-coil dimer domain of C. reinhardtii SAS-6 homolog Bld12p== | ||
<StructureSection load='3q0x' size='340' side='right'caption='[[3q0x]], [[Resolution|resolution]] 3.02Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3q0x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q0X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q0X FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.02Å</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=3q0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q0x OCA], [https://pdbe.org/3q0x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q0x RCSB], [https://www.ebi.ac.uk/pdbsum/3q0x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q0x ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A9CQL4_CHLRE A9CQL4_CHLRE] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The centriole, and the related basal body, is an ancient organelle characterized by a universal 9-fold radial symmetry and is critical for generating cilia, flagella, and centrosomes. The mechanisms directing centriole formation are incompletely understood and represent a fundamental open question in biology. Here, we demonstrate that the centriolar protein SAS-6 forms rod-shaped homodimers that interact through their N-terminal domains to form oligomers. We establish that such oligomerization is essential for centriole formation in C. elegans and human cells. We further generate a structural model of the related protein Bld12p from C. reinhardtii, in which nine homodimers assemble into a ring from which nine coiled-coil rods radiate outward. Moreover, we demonstrate that recombinant Bld12p self-assembles into structures akin to the central hub of the cartwheel, which serves as a scaffold for centriole formation. Overall, our findings establish a structural basis for the universal 9-fold symmetry of centrioles. | |||
Structural basis of the 9-fold symmetry of centrioles.,Kitagawa D, Vakonakis I, Olieric N, Hilbert M, Keller D, Olieric V, Bortfeld M, Erat MC, Fluckiger I, Gonczy P, Steinmetz MO Cell. 2011 Feb 4;144(3):364-75. PMID:21277013<ref>PMID:21277013</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3q0x" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Chlamydomonas reinhardtii]] | |||
[[Category: Large Structures]] | |||
[[Category: Bortfeld M]] | |||
[[Category: Erat MC]] | |||
[[Category: Flueckiger I]] | |||
[[Category: Goenczy P]] | |||
[[Category: Hilbert M]] | |||
[[Category: Keller D]] | |||
[[Category: Kitagawa D]] | |||
[[Category: Olieric N]] | |||
[[Category: Olieric V]] | |||
[[Category: Steinmetz MO]] | |||
[[Category: Vakonakis I]] | |||
Latest revision as of 08:06, 9 October 2024
N-terminal coiled-coil dimer domain of C. reinhardtii SAS-6 homolog Bld12p
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