View source for 8s35


==DNA-bound Type IV-A3 CRISPR effector in complex with DinG helicase from K. pneumoniae (state I)==
<StructureSection load='8s35' size='340' side='right'caption='[[8s35]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8s35]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8S35 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8S35 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]] 2.9&#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=8s35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8s35 OCA], [https://pdbe.org/8s35 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8s35 RCSB], [https://www.ebi.ac.uk/pdbsum/8s35 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8s35 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A333ESG5_KLEPN A0A333ESG5_KLEPN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
CRISPR-Cas mediated DNA-interference typically relies on sequence-specific binding and nucleolytic degradation of foreign genetic material. Type IV-A CRISPR-Cas systems diverge from this general mechanism, using a nuclease-independent interference pathway to suppress gene expression for gene regulation and plasmid competition. To understand how the type IV-A system associated effector complex achieves this interference, we determine cryo-EM structures of two evolutionarily distinct type IV-A complexes (types IV-A1 and IV-A3) bound to cognate DNA-targets in the presence and absence of the type IV-A signature DinG effector helicase. The structures reveal how the effector complexes recognize the protospacer adjacent motif and target-strand DNA to form an R-loop structure. Additionally, we reveal differences between types IV-A1 and IV-A3 in DNA interactions and structural motifs that allow for in trans recruitment of DinG. Our study provides a detailed view of type IV-A mediated DNA-interference and presents a structural foundation for engineering type IV-A-based genome editing tools.

Structural variation of types IV-A1- and IV-A3-mediated CRISPR interference.,Cepaite R, Klein N, Miksys A, Camara-Wilpert S, Ragozius V, Benz F, Skorupskaite A, Becker H, Zvejyte G, Steube N, Hochberg GKA, Randau L, Pinilla-Redondo R, Malinauskaite L, Pausch P Nat Commun. 2024 Oct 29;15(1):9306. doi: 10.1038/s41467-024-53778-1. PMID:39468082<ref>PMID:39468082</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8s35" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Klebsiella pneumoniae]]
[[Category: Large Structures]]
[[Category: Cepaite R]]
[[Category: Klein N]]
[[Category: Malinauskaite L]]
[[Category: Pausch P]]
[[Category: Ragozius V]]
[[Category: Randau L]]
[[Category: Skorupskaite A]]