9y66: Difference between revisions

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'''Unreleased structure'''


The entry 9y66 is ON HOLD  until Paper Publication
==attLsym bound serine integrase complex in the dimeric state==
<StructureSection load='9y66' size='340' side='right'caption='[[9y66]], [[Resolution|resolution]] 3.31&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9y66]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_virus_SPbeta Bacillus virus SPbeta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9Y66 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9Y66 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]] 3.31&#8491;</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=9y66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9y66 OCA], [https://pdbe.org/9y66 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9y66 RCSB], [https://www.ebi.ac.uk/pdbsum/9y66 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9y66 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Large serine integrases (LSIs) catalyze unidirectional site-specific DNA recombination reactions, yet those reactions are reversed by the presence of a cognate recombination directionality factor (RDF). Mechanistic understanding of directionality control has been hampered by a lack of structural information. Here, we use cryo-electron microscopy (cryo-EM) to determine the structures of six SPbeta integrase-DNA complexes along the integrative (-RDF) and excisive (+RDF) reaction pathways, at 4.16-7.18A resolution. Our findings reveal how RDF-mediated repositioning of an integrase subdomain (1) dictates which pairs of DNA sites can be assembled into a synaptic complex to initiate recombination and (2) dictates which product complexes will be conformationally locked, preventing the back reaction. These mechanistic insights provide a conceptual framework for engineering efficient and versatile genome editing tools.


Authors:  
Structural basis of directionality control in large serine integrases.,Shin H, Pigli Y, Reyes TP, Fuller JR, Olorunniji FJ, Rice PA bioRxiv [Preprint]. 2025 Jan 13:2025.01.03.631226. doi: , 10.1101/2025.01.03.631226. PMID:39803483<ref>PMID:39803483</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 9y66" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus virus SPbeta]]
[[Category: Large Structures]]
[[Category: Fuller JR]]
[[Category: Olorunniji FJ]]
[[Category: Pena Reyes T]]
[[Category: Pigli Y]]
[[Category: Rice PA]]
[[Category: Shin H]]

Latest revision as of 19:36, 10 February 2026

attLsym bound serine integrase complex in the dimeric state

9y66, resolution 3.31Å

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