8at2
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8at2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AT2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AT2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[8at2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AT2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AT2 FirstGlance]. <br> | ||
| - | </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=8at2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8at2 OCA], [https://pdbe.org/8at2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8at2 RCSB], [https://www.ebi.ac.uk/pdbsum/8at2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8at2 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 7.7Å</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=8at2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8at2 OCA], [https://pdbe.org/8at2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8at2 RCSB], [https://www.ebi.ac.uk/pdbsum/8at2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8at2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | [https://www.uniprot.org/uniprot/ | + | [https://www.uniprot.org/uniprot/A0A8J1L9M8_XENLA A0A8J1L9M8_XENLA] |
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | In mitosis, the augmin complex binds to spindle microtubules to recruit the gamma-tubulin ring complex (gamma-TuRC), the principal microtubule nucleator, for the formation of branched microtubules. Our understanding of augmin-mediated microtubule branching is hampered by the lack of structural information on the augmin complex. Here, we elucidate the molecular architecture and conformational plasticity of the augmin complex using an integrative structural biology approach. The elongated structure of the augmin complex is characterised by extensive coiled-coil segments and comprises two structural elements with distinct but complementary functions in gamma-TuRC and microtubule binding, linked by a flexible hinge. The augmin complex is recruited to microtubules via a composite microtubule binding site comprising a positively charged unordered extension and two calponin homology domains. Our study provides the structural basis for augmin function in branched microtubule formation, decisively fostering our understanding of spindle formation in mitosis. | ||
| + | |||
| + | The augmin complex architecture reveals structural insights into microtubule branching.,Zupa E, Wurtz M, Neuner A, Hoffmann T, Rettel M, Bohler A, Vermeulen BJA, Eustermann S, Schiebel E, Pfeffer S Nat Commun. 2022 Sep 26;13(1):5635. doi: 10.1038/s41467-022-33228-6. PMID:36163468<ref>PMID:36163468</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8at2" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Structure of the augmin TIII subcomplex
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