6p5a: Difference between revisions

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 <StructureSection load='6p5a' size='340' side='right'caption='[[6p5a]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6p5a]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P5A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6P5A FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6p5a]] 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=6P5A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6P5A FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6p5a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p5a OCA], [http://pdbe.org/6p5a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6p5a RCSB], [http://www.ebi.ac.uk/pdbsum/6p5a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6p5a ProSAT]</span></td></tr>
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 == 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>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
+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>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 6p5a" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Drome]]
 [[Category: Large Structures]]
 [[Category: Ghanim, G]]