View source for 9vtr


==Target DNA-bound type I-F3 TniQ-Cascade of Vibrio parahaemolyticus in full R-loop state 2==
<StructureSection load='9vtr' size='340' side='right'caption='[[9vtr]], [[Resolution|resolution]] 2.89&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9vtr]] is a 13 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_parahaemolyticus_RIMD_2210633 Vibrio parahaemolyticus RIMD 2210633]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9VTR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9VTR 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]] 2.89&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=9vtr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9vtr OCA], [https://pdbe.org/9vtr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9vtr RCSB], [https://www.ebi.ac.uk/pdbsum/9vtr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9vtr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q87GC7_VIBPA Q87GC7_VIBPA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Some prokaryotes carry CRISPR-associated transposons (CASTs), Tn7-like elements that incorporate genes encoding CRISPR-Cas effectors. CAST insertion is directed by CRISPR-Cas effectors through RNA-guided DNA binding and interactions with transposition-associated proteins. Although efficient sequence-specific DNA integration requires both precise target DNA recognition and coordinated interactions between effectors and transposition-associated proteins, the underlying mechanism remains elusive. Here, we determined three cryo-EM structures of target DNA-bound type I-F3 TniQ-Cascade from Vibrio parahaemolyticus, revealing how Cas8/5 recognizes the protospacer adjacent motif (PAM) and identifying a key residue responsible for the cytidine preference at position -2 of the PAM. We revealed mismatch tolerance at the PAM-proximal site. Structural analyses showed that correct base pairing at the PAM-distal site correlates with conformational changes in the Cas8/5 helical bundle and TniQ, bending the DNA to guide its downstream region toward the transposition machinery. Together, these dynamic rearrangements at the PAM-distal region provide insights into the licensing mechanism of type I-F3 CAST transposition and highlight its potential for genome engineering applications.

Sequential structural rearrangements at the PAM-distal site of a type I-F3 CRISPR-Cas effector enabling RNA-guided DNA transposition.,Ishihara K, Matsumoto S, Gerle C, Gopalasingam CC, Shigematsu H, Shirai T, Numata T Nucleic Acids Res. 2026 Jan 5;54(1):gkaf1415. doi: 10.1093/nar/gkaf1415. PMID:41495894<ref>PMID:41495894</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9vtr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Vibrio parahaemolyticus RIMD 2210633]]
[[Category: Ishihara K]]
[[Category: Numata T]]