8sjd: Difference between revisions
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New page: '''Unreleased structure''' The entry 8sjd is ON HOLD Authors: Lannes, L., Dyda, F. Description: Cryo-EM structure of the Hermes transposase bound to two right-ends of its DNA transposo... |
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The | ==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]] 5.10Å' 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]] 5.1Å</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. | |||
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 8sjd" style="background-color:#fffaf0;"></div> | ||
[[Category: Lannes | |||
==See Also== | |||
*[[Transposase 3D structures|Transposase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Musca domestica]] | |||
[[Category: Dyda F]] | |||
[[Category: Lannes L]] | |||
Latest revision as of 09:58, 19 June 2024
Cryo-EM structure of the Hermes transposase bound to two right-ends of its DNA transposon.Cryo-EM structure of the Hermes transposase bound to two right-ends of its DNA transposon.
Structural highlights
FunctionPublication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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