6M3N

Solution structure of anti-CRISPR AcrIF7

Summary for 6M3N

• Entry DOI: 10.2210/pdb6m3n/pdb
• NMR Information: BMRB: 36320
• Descriptor: anti-CRIPSR AcrIF7 (1 entity in total)
• Functional Keywords: anti-crispr inhibitor, hydrolase inhibitor
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 1
• Total formula weight: 7526.07

Authors

Kim, I.,An, S.Y.,Koo, J.,Bae, E.,Suh, J.Y. (deposition date: 2020-03-04, release date: 2020-08-26, Last modification date: 2024-05-15)

Primary citation

Kim, I.,Koo, J.,An, S.Y.,Hong, S.,Ka, D.,Kim, E.H.,Bae, E.,Suh, J.Y.
Structural and mechanistic insights into the CRISPR inhibition of AcrIF7.
Nucleic Acids Res., 48:9959-9968, 2020

PubMed Abstract: The CRISPR-Cas system provides adaptive immunity for bacteria and archaea to combat invading phages and plasmids. Phages evolved anti-CRISPR (Acr) proteins to neutralize the host CRISPR-Cas immune system as a counter-defense mechanism. AcrIF7 in Pseudomonas aeruginosa prophages strongly inhibits the type I-F CRISPR-Cas system. Here, we determined the solution structure of AcrIF7 and identified its target, Cas8f of the Csy complex. AcrIF7 adopts a novel β1β2α1α2β3 fold and interacts with the target DNA binding site of Cas8f. Notably, AcrIF7 competes with AcrIF2 for the same binding interface on Cas8f without common structural motifs. AcrIF7 binding to Cas8f is driven mainly by electrostatic interactions that require position-specific surface charges. Our findings suggest that Acrs of divergent origin may have acquired specificity to a common target through convergent evolution of their surface charge configurations.

PubMed: 32810226
DOI: 10.1093/nar/gkaa690

Experimental method

SOLUTION NMR