View source for 30jv


==Cryo-EM structure of the PseTnsAB paired-end complex (right end) in the presence of Mn==
<StructureSection load='30jv' size='340' side='right'caption='[[30jv]], [[Resolution|resolution]] 2.86&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[30jv]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudoalteromonas_sp._S983 Pseudoalteromonas sp. S983]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=30JV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=30JV 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]] 2.86&#8491;</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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=30jv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=30jv OCA], [https://pdbe.org/30jv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=30jv RCSB], [https://www.ebi.ac.uk/pdbsum/30jv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=30jv ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
CRISPR-associated transposons (CASTs) are Tn7-like elements that have co-opted RNA-guided CRISPR effectors for targeted DNA insertion. CASTs have been adapted as genome editing tools for programmable, site-specific integration. Among them, the type I-F system from Ps e udoalteromonas ( Pse CAST) shows uniquely robust activity in human cells, yet its mechanistic basis remains poorly understood. Here, we present structural and biochemical analysis of the Pse CAST transposase TnsAB. Biochemical reconstitution of transposon DNA excision defines key characteristics of the transposition mechanism. Cryogenic electron microscopy (cryo-EM) structures of Pse TnsAB paired-end complexes reveal molecular determinants of transpososome assembly, transposon end recognition and cleavage. We validate these findings using biochemical and in vivo assays of structure-based transposase mutants, and provide mechanistic insights into the enhanced activity of a laboratory-evolved TnsAB variant. Together, our studies highlight molecular features underlying the efficiency of natural and engineered type I-F transposases and establish a mechanistic framework for their continued rational optimization.

Transposon end recognition and excision mechanisms of type I-F CRISPR-associated transposases.,Walter M, Finocchio G, Oberli S, Hammerschmid IC, Lampe GD, Karan J, Swartjes T, Sternberg SH, Jinek M, Querques I bioRxiv [Preprint]. 2026 May 7:2026.05.05.722991. doi: , 10.64898/2026.05.05.722991. PMID:42146515<ref>PMID:42146515</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 30jv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudoalteromonas sp. S983]]
[[Category: Finocchio G]]
[[Category: Jinek M]]
[[Category: Oberli S]]