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6pe2

From Proteopedia

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Current revision (09:26, 20 March 2024) (edit) (undo)
 
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<SX load='6pe2' size='340' side='right' viewer='molstar' caption='[[6pe2]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
<SX load='6pe2' size='340' side='right' viewer='molstar' caption='[[6pe2]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<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>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6p5a|6p5a]]</td></tr>
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<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>
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<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>
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<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 ==
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[[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>
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[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>
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<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&reg;/PubMed&reg;, 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>
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[[Category: Drome]]
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[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Ghanim, G]]
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[[Category: Ghanim G]]
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[[Category: Kellogg, E H]]
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[[Category: Kellogg EH]]
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[[Category: Nogales, E]]
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[[Category: Nogales E]]
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[[Category: Rio, D C]]
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[[Category: Rio DC]]
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[[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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Current revision

Drosophila P element transposase strand transfer complex

6pe2, resolution 4.00Å

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