Structural highlights
Function
A0A377JKY9_HAEPA
Publication Abstract from PubMed
Phages, plasmids, and other mobile genetic elements express inhibitors of CRISPR-Cas immune systems, known as anti-CRISPR proteins, to protect themselves from targeted destruction. These anti-CRISPR proteins have been shown to function through very diverse mechanisms. In this work we investigate the activity of an anti-CRISPR isolated from a prophage in Haemophilus parainfluenzae that blocks CRISPR-Cas9 DNA cleavage activity. We determine the three-dimensional crystal structure of AcrIIC4Hpa and show that it binds to the Cas9 Recognition Domain. This binding does not prevent the Cas9-anti-CRISPR complex from interacting with target DNA but does inhibit DNA cleavage. AcrIIC4Hpa likely acts by blocking the conformational changes that allow the HNH and RuvC endonuclease domains to contact the DNA sites to be nicked.
Structural and Mechanistic Insight into CRISPR-Cas9 Inhibition by Anti-CRISPR Protein AcrIIC4Hpa.,Hwang S, Pan C, Garcia B, Davidson AR, Moraes TF, Maxwell KL J Mol Biol. 2022 Mar 15;434(5):167420. doi: 10.1016/j.jmb.2021.167420. Epub 2021 , Dec 23. PMID:34954237[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hwang S, Pan C, Garcia B, Davidson AR, Moraes TF, Maxwell KL. Structural and Mechanistic Insight into CRISPR-Cas9 Inhibition by Anti-CRISPR Protein AcrIIC4(Hpa). J Mol Biol. 2022 Mar 15;434(5):167420. PMID:34954237 doi:10.1016/j.jmb.2021.167420
