View source for 7sqk


==Cryo-EM structure of the human augmin complex==
<StructureSection load='7sqk' size='340' side='right'caption='[[7sqk]], [[Resolution|resolution]] 8.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7sqk]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SQK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SQK 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]] 8&#8491;</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=7sqk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7sqk OCA], [https://pdbe.org/7sqk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7sqk RCSB], [https://www.ebi.ac.uk/pdbsum/7sqk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7sqk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HAUS1_HUMAN HAUS1_HUMAN] Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex.<ref>PMID:15082789</ref> <ref>PMID:19369198</ref> <ref>PMID:19427217</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Accurate segregation of chromosomes during mitosis depends on the correct assembly of the mitotic spindle, a bipolar structure composed mainly of microtubules. The augmin complex, or homologous to augmin subunits (HAUS) complex, is an eight-subunit protein complex required for building robust mitotic spindles in metazoa. Augmin increases microtubule density within the spindle by recruiting the gamma-tubulin ring complex (gamma-TuRC) to pre-existing microtubules and nucleating branching microtubules. Here, we elucidate the molecular architecture of augmin by single particle cryo-electron microscopy (cryo-EM), computational methods, and crosslinking mass spectrometry (CLMS). Augmin's highly flexible structure contains a V-shaped head and a filamentous tail, with the head existing in either extended or contracted conformational states. Our work highlights how cryo-EM, complemented by computational advances and CLMS, can elucidate the structure of a challenging protein complex and provides insights into the function of augmin in mediating microtubule branching nucleation.

Molecular architecture of the augmin complex.,Gabel CA, Li Z, DeMarco AG, Zhang Z, Yang J, Hall MC, Barford D, Chang L Nat Commun. 2022 Sep 16;13(1):5449. doi: 10.1038/s41467-022-33227-7. PMID:36114186<ref>PMID:36114186</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7sqk" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Chang L]]
[[Category: Gabel CA]]