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| <SX load='6pe2' size='340' side='right' viewer='molstar' caption='[[6pe2]], [[Resolution|resolution]] 4.00Å' scene=''> | | <SX load='6pe2' size='340' side='right' viewer='molstar' caption='[[6pe2]], [[Resolution|resolution]] 4.00Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[6pe2]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PE2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6PE2 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[6pe2]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PE2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PE2 FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6p5a|6p5a]]</td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6pe2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pe2 OCA], [http://pdbe.org/6pe2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pe2 RCSB], [http://www.ebi.ac.uk/pdbsum/6pe2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pe2 ProSAT]</span></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=6pe2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pe2 OCA], [https://pdbe.org/6pe2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pe2 RCSB], [https://www.ebi.ac.uk/pdbsum/6pe2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pe2 ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/PELET_DROME PELET_DROME]] P-element transposase that specifically mediates transposition of P-elements. Mediates both; precise and imprecise excision.<ref>PMID:2416475</ref> <ref>PMID:20010837</ref> | | [https://www.uniprot.org/uniprot/PELET_DROME PELET_DROME] P-element transposase that specifically mediates transposition of P-elements. Mediates both; precise and imprecise excision.<ref>PMID:2416475</ref> <ref>PMID:20010837</ref> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| P element transposase catalyzes the mobility of P element DNA transposons within the Drosophila genome. P element transposase exhibits several unique properties, including the requirement for a guanosine triphosphate cofactor and the generation of long staggered DNA breaks during transposition. To gain insights into these features, we determined the atomic structure of the Drosophila P element transposase strand transfer complex using cryo-EM. The structure of this post-transposition nucleoprotein complex reveals that the terminal single-stranded transposon DNA adopts unusual A-form and distorted B-form helical geometries that are stabilized by extensive protein-DNA interactions. Additionally, we infer that the bound guanosine triphosphate cofactor interacts with the terminal base of the transposon DNA, apparently to position the P element DNA for catalysis. Our structure provides the first view of the P element transposase superfamily, offers new insights into P element transposition and implies a transposition pathway fundamentally distinct from other cut-and-paste DNA transposases.
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| Structure of a P element transposase-DNA complex reveals unusual DNA structures and GTP-DNA contacts.,Ghanim GE, Kellogg EH, Nogales E, Rio DC Nat Struct Mol Biol. 2019 Oct 28. pii: 10.1038/s41594-019-0319-6. doi:, 10.1038/s41594-019-0319-6. PMID:31659330<ref>PMID:31659330</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 6pe2" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
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| __TOC__ | | __TOC__ |
| </SX> | | </SX> |
| [[Category: Drome]] | | [[Category: Drosophila melanogaster]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Ghanim, G]] | | [[Category: Ghanim G]] |
| [[Category: Kellogg, E H]] | | [[Category: Kellogg EH]] |
| [[Category: Nogales, E]] | | [[Category: Nogales E]] |
| [[Category: Rio, D C]] | | [[Category: Rio DC]] |
| [[Category: Strand transfer complex]]
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| [[Category: Transferase-dna]]
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| [[Category: Transferase-dna complex]]
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| [[Category: Transposase]]
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