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TitleStructural basis for dual mechanism of Cas2/3 nuclease inhibition by anti-CRISPR protein AcrIF19.
Journal, issue, pagesNat Commun, Vol. 17, Issue 1, Year 2026
Publish dateMay 19, 2026
AuthorsYuanshuo Sa / Chunlei Liu / Lingguang Yang / Ling Yue / Limin Zhu / Ying Guo / Ruimei Wang / Yafei Wang / Yue Feng / Yong Wang / Yi Zhang / Wenhe Wang / Yongchao Xie /
PubMed AbstractCRISPR-Cas systems are prokaryotic immune mechanisms often targeted by phage-encoded anti-CRISPR (Acr) proteins. This study characterizes AcrIF19, a potent inhibitor of the type I-F system in ...CRISPR-Cas systems are prokaryotic immune mechanisms often targeted by phage-encoded anti-CRISPR (Acr) proteins. This study characterizes AcrIF19, a potent inhibitor of the type I-F system in Pectobacterium atrosepticum. The cryo-EM structure of the apo Cas2/3 and Cas2/3-AcrIF19 complex reveals a dual inhibitory mechanism. AcrIF19 employs a negatively charged β-β loop to sterically occlude the non-target DNA strand entry channel, acting as a competitive inhibitor to disrupt Cas2/3 recruitment. Concurrently, this steric occlusion impedes ssDNA-mediated allosteric activation, which locks the critical helix-like loop motif in an inhibitory conformation and thereby abrogates DNA cleavage activity. AcrIF19 represents an anti-CRISPR protein inhibiting Cas2/3 via two different mechanisms, integrating a competitive ssDNA inhibitor with an allosteric blockade to suppress both target recruitment and DNA cleavage.
External linksNat Commun / PubMed:42156407 / PubMed Central
MethodsEM (single particle)
Resolution2.55 - 2.97 Å
Structure data

66478

9x2f

EMDB-66478, PDB-9x2f:
complex of anti-CRISPR Protein
Method: EM (single particle) / Resolution: 2.97 Å

68883

23dj

EMDB-68883, PDB-23dj:
anti-Crispr protein in apo form
Method: EM (single particle) / Resolution: 2.55 Å

Chemicals

ChemComp-NI:
NICKEL (II) ION

Source
  • pectobacterium araliae (bacteria)
KeywordsCELL INVASION / anti-Crispr protein in apo form / PROTEIN BINDING / complex of anti-CRISPR Protein

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