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8edg
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Cryo-EM structure of the Hermes transposase bound to two left-ends of its DNA transposon== | |
| + | <StructureSection load='8edg' size='340' side='right'caption='[[8edg]], [[Resolution|resolution]] 4.64Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8edg]] is a 12 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=8EDG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8EDG 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]] 4.64Å</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=8edg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8edg OCA], [https://pdbe.org/8edg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8edg RCSB], [https://www.ebi.ac.uk/pdbsum/8edg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8edg 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Dyda | + | <div class="pdbe-citations 8edg" style="background-color:#fffaf0;"></div> |
| - | [[Category: Lannes | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Musca domestica]] | ||
| + | [[Category: Dyda F]] | ||
| + | [[Category: Lannes L]] | ||
Current revision
Cryo-EM structure of the Hermes transposase bound to two left-ends of its DNA transposon
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