9c0f
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==piggyBat transposase protein-DNA complex== | |
| + | <StructureSection load='9c0f' size='340' side='right'caption='[[9c0f]], [[Resolution|resolution]] 3.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9c0f]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Myotis_lucifugus Myotis lucifugus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9C0F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9C0F 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]] 3.6Å</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=9c0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9c0f OCA], [https://pdbe.org/9c0f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9c0f RCSB], [https://www.ebi.ac.uk/pdbsum/9c0f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9c0f ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Members of the piggyBac superfamily of DNA transposons are widely distributed in host genomes ranging from insects to mammals. The human genome has retained five piggyBac-derived genes as domesticated elements although they are no longer mobile. Here, we have investigated the transposition properties of piggyBat from Myotis lucifugus, the only known active mammalian DNA transposon, and show that its low activity in human cells is due to subterminal inhibitory DNA sequences. Activity can be dramatically improved by their removal, suggesting the existence of a mechanism for the suppression of transposon activity. The cryo-electron microscopy structure of the piggyBat transposase pre-synaptic complex showed an unexpected mode of DNA binding and recognition using C-terminal domains that are topologically different from those of the piggyBac transposase. Here we show that structure-based rational re-engineering of the transposase through the removal of putative phosphorylation sites and a changed domain organization - in combination with truncated transposon ends - results in a transposition system that is at least 100-fold more active than wild-type piggyBat. | ||
| - | + | Activity of the mammalian DNA transposon piggyBat from Myotis lucifugus is restricted by its own transposon ends.,Hickman AB, Lannes L, Furman CM, Hong C, Franklin L, Ghirlando R, Ghosh A, Luo W, Konstantinidou P, Lorenzi HA, Grove A, Haase AD, Wilson MH, Dyda F Nat Commun. 2025 Jan 7;16(1):458. doi: 10.1038/s41467-024-55784-9. PMID:39774116<ref>PMID:39774116</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 9c0f" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Myotis lucifugus]] | ||
| + | [[Category: Dyda F]] | ||
| + | [[Category: Hickman AB]] | ||
| + | [[Category: Lannes L]] | ||
Current revision
piggyBat transposase protein-DNA complex
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