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9SVK

cryo-EM structure of LwHicAB-crRNA

Summary for 9SVK
Entry DOI10.2210/pdb9svk/pdb
EMDB information55261
DescriptorToxin-antitoxin system, antitoxin component, HicB family, Toxin-antitoxin system, toxin component, HicA family, RNA (58-MER) (3 entities in total)
Functional Keywordstoxin-antitoxin, crispr rna binding, prokaryotic immunity, immune system
Biological sourceLeptotrichia wadei F0279
More
Total number of polymer chains14
Total formula weight193024.27
Authors
Liang, L.,Jiyun, C.,Xueyan, L. (deposition date: 2025-10-03, release date: 2026-09-09)
Primary citationChen, J.,Huang, L.,Chen, H.,Li, X.,Lin, X.,Guo, C.,Liu, X.,Fu, G.,Chen, Y.,Liu, L.
Potential role of a CRISPR-Cas-activated toxin-antitoxin system in bacterial immunity.
Nat Commun, 17:-, 2026
Cited by
PubMed Abstract: CRISPR-Cas and toxin-antitoxin systems can serve as antiviral defense mechanisms in prokaryotes. In typical toxin-antitoxin systems, toxin activation can limit phage propagation by inducing growth arrest or reduced cellular fitness, while the antitoxin neutralizes toxin activity. Here, we study potential functional synergy between a CRISPR-Cas13a system and a type II toxin-antitoxin module (HicAB) from a Leptotrichia bacterium, when heterologously expressed in E. coli, as well as in biochemical and structural analyses. We show that the antitoxin HicB exhibits toxic properties, and Cas13a directly activates HicB, triggering growth inhibition and conferring protection against bacteriophages. Structural analyses reveal that Cas13a binding promotes the spatial proximity of HicB tetramers, likely enabling its activation. The toxin HicA competitively binds to HicB, thereby inhibiting Cas13a-mediated HicB activation. Importantly, both CRISPR RNA and HicB independently suppress HicA toxicity. Structural evidence indicates that CRISPR RNA forms a hetero-tetradecameric complex with HicAB, occluding HicA's active site and neutralizing its toxic function. Thus, our findings indicate functional synergy between distinct bacterial immune strategies.
PubMed: 42362581
DOI: 10.1038/s41467-026-74930-z
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.4 Å)
Structure validation

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PDB entries from 2026-09-09

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