6dww: Difference between revisions
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<StructureSection load='6dww' size='340' side='right'caption='[[6dww]], [[Resolution|resolution]] 2.85Å' scene=''> | <StructureSection load='6dww' size='340' side='right'caption='[[6dww]], [[Resolution|resolution]] 2.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6dww]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6dww]] is a 4 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=6DWW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DWW FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.851Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=6dww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dww OCA], [https://pdbe.org/6dww PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6dww RCSB], [https://www.ebi.ac.uk/pdbsum/6dww PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6dww ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q25438_MUSDO Q25438_MUSDO] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Musca domestica]] | ||
[[Category: | [[Category: Dyda F]] | ||
[[Category: | [[Category: Hickman AB]] | ||
[[Category: | [[Category: Voth AR]] | ||
Latest revision as of 09:15, 11 October 2023
Hermes transposase deletion dimer complex with (A/T) DNA and Mn2+Hermes transposase deletion dimer complex with (A/T) DNA and Mn2+
Structural highlights
FunctionPublication Abstract from PubMedSome DNA transposons relocate from one genomic location to another using a mechanism that involves generating double-strand breaks at their transposon ends by forming hairpins on flanking DNA. The same double-strand break mode is employed by the V(D)J recombinase at signal-end/coding-end junctions during the generation of antibody diversity. How flanking hairpins are formed during DNA transposition has remained elusive. Here, we describe several co-crystal structures of the Hermes transposase bound to DNA that mimics the reaction step immediately prior to hairpin formation. Our results reveal a large DNA conformational change between the initial cleavage step and subsequent hairpin formation that changes which strand is acted upon by a single active site. We observed that two factors affect the conformational change: the complement of divalent metal ions bound by the catalytically essential DDE residues, and the identity of the -2 flanking base pair. Our data also provides a mechanistic link between the efficiency of hairpin formation (an A:T basepair is favored at the -2 position) and Hermes' strong target site preference. Furthermore, we have established that the histidine residue within a conserved C/DxxH motif present in many transposase families interacts directly with the scissile phosphate, suggesting a crucial role in catalysis. Structural insights into the mechanism of double strand break formation by Hermes, a hAT family eukaryotic DNA transposase.,Hickman AB, Voth AR, Ewis H, Li X, Craig NL, Dyda F Nucleic Acids Res. 2018 Nov 2;46(19):10286-10301. doi: 10.1093/nar/gky838. PMID:30239795[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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