8eb5: Difference between revisions

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'''Unreleased structure'''


The entry 8eb5 is ON HOLD
==Tandem of Hermes transposase BED domain in complex with the quasi palindrome of its transposon left-end==
<StructureSection load='8eb5' size='340' side='right'caption='[[8eb5]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8eb5]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Musca_domestica Musca domestica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8EB5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8EB5 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]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=8eb5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8eb5 OCA], [https://pdbe.org/8eb5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8eb5 RCSB], [https://www.ebi.ac.uk/pdbsum/8eb5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8eb5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q25442_MUSDO Q25442_MUSDO]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Hermes DNA transposon is a member of the eukaryotic hAT superfamily, and its transposase forms a ring-shaped tetramer of dimers. Our investigation, combining biochemical, crystallography and cryo-electron microscopy, and in-cell assays, shows that the full-length Hermes octamer extensively interacts with its transposon left-end through multiple BED domains of three Hermes protomers contributed by three dimers explaining the role of the unusual higher-order assembly. By contrast, the right-end is bound to no BED domains at all. Thus, this work supports a model in which Hermes multimerizes to gather enough BED domains to find its left-end among the abundant genomic DNA, facilitating the subsequent interaction with the right-end.


Authors: Lannes, L., Dyda, F.
Zinc-finger BED domains drive the formation of the active Hermes transpososome by asymmetric DNA binding.,Lannes L, Furman CM, Hickman AB, Dyda F Nat Commun. 2023 Jul 25;14(1):4470. doi: 10.1038/s41467-023-40210-3. PMID:37491363<ref>PMID:37491363</ref>


Description: Tandem of Hermes transposase BED domain in complex with the quasi palindrome of its transposon left-end
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Dyda, F]]
<div class="pdbe-citations 8eb5" style="background-color:#fffaf0;"></div>
[[Category: Lannes, L]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Musca domestica]]
[[Category: Dyda F]]
[[Category: Lannes L]]