9w6c: Difference between revisions
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==Crystal structure of Cas5IC from Moraxella bovoculi== | |||
<StructureSection load='9w6c' size='340' side='right'caption='[[9w6c]], [[Resolution|resolution]] 3.33Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9w6c]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Moraxella_bovoculi Moraxella bovoculi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9W6C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9W6C FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.33Å</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=9w6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9w6c OCA], [https://pdbe.org/9w6c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9w6c RCSB], [https://www.ebi.ac.uk/pdbsum/9w6c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9w6c ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
CRISPR-Cas systems are essential for prokaryotic adaptive immune mechanisms; however, the structural details of many subtype-specific components remain unclear. Herein, we report the crystal structure and biophysical characterization of Cas5 from Moraxella bovoculi (MboCas5), a component of the type I-C CRISPR-Cas system. We found that M. bovoculi encodes both type I-C and type III-B systems, and that MboCas5 forms a dimer that is stabilized by key interactions, including a salt bridge between R72 and D167. Structural comparisons with other Cas5 homologs and AlphaFold 3 predictions further validated the unique dimer configuration, suggesting that it is conserved across species. Additionally, structural comparison revealed a highly flexible loop region, which likely undergoes conformational changes upon Cascade assembly and might mediate interactions with Cas8 and crRNA. Overall, the findings provided structural and mechanistic insights into Cas5 function and could potentially contribute to our understanding of the assembly of type I-C Cascade complexes. | |||
Structural basis of dimerization and cascade formation by Cas5.,Kang YJ, Ha HJ, Jin HB, Lee SY, Park HH Sci Rep. 2025 Dec 15;16(1):2976. doi: 10.1038/s41598-025-32766-5. PMID:41398311<ref>PMID:41398311</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 9w6c" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Moraxella bovoculi]] | |||
[[Category: Kang YJ]] | |||
[[Category: Park HH]] | |||
Latest revision as of 07:25, 17 June 2026
Crystal structure of Cas5IC from Moraxella bovoculi
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