8sjd: Difference between revisions

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-'''Unreleased structure'''
-The entry 8sjd is ON HOLD  until Paper Publication
+==Cryo-EM structure of the Hermes transposase bound to two right-ends of its DNA transposon.==
+<StructureSection load='8sjd' size='340' side='right'caption='[[8sjd]], [[Resolution|resolution]] 5.10&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8sjd]] is a 10 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=8SJD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8SJD 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]] 5.1&#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=8sjd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8sjd OCA], [https://pdbe.org/8sjd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8sjd RCSB], [https://www.ebi.ac.uk/pdbsum/8sjd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8sjd ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q25438_MUSDO Q25438_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: Cryo-EM structure of the Hermes transposase bound to two right-ends of its DNA transposon.
+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 8sjd" style="background-color:#fffaf0;"></div>
-[[Category: Lannes, L]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Musca domestica]]
+[[Category: Dyda F]]
+[[Category: Lannes L]]