8IA4
Crystal structure of Cas2 in complex with AcrVA5-peptide
Summary for 8IA4
| Entry DOI | 10.2210/pdb8ia4/pdb |
| Descriptor | CRISPR-associated endoribonuclease Cas2, peptide (3 entities in total) |
| Functional Keywords | crispr-cas, integration, cas2, gene regulation |
| Biological source | Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104) More |
| Total number of polymer chains | 3 |
| Total formula weight | 24107.17 |
| Authors | |
| Primary citation | Bi, M.,Su, W.,Li, J.,Mo, X. Insights into the inhibition of protospacer integration via direct interaction between Cas2 and AcrVA5. Nat Commun, 15:3256-3256, 2024 Cited by PubMed Abstract: Spacer acquisition step in CRISPR-Cas system involves the recognition and subsequent integration of protospacer by the Cas1-Cas2 complex in CRISPR-Cas systems. Here we report an anti-CRISPR protein, AcrVA5, and reveal the mechanisms by which it strongly inhibits protospacer integration. Our biochemical data shows that the integration by Cas1-Cas2 was abrogated in the presence of AcrVA5. AcrVA5 exhibits low binding affinity towards Cas2 and acetylates Cas2 at Lys on the binding interface of the Cas2 and AcrVA5 N-terminal peptide complex to inhibit the Cas2-mediated endonuclease activity. Moreover, a detailed structural comparison between our crystal structure and homolog structure shows that binding of AcrVA5 to Cas2 causes steric hindrance to the neighboring protospacer resulting in the partial disassembly of the Cas1-Cas2 and protospacer complex, as demonstrated by electrophoretic mobility shift assay. Our study focuses on this mechanism of spacer acquisition inhibition and provides insights into the biology of CRISPR-Cas systems. PubMed: 38627399DOI: 10.1038/s41467-024-47713-7 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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