7MSL
Structure of anti-CRISPR AcrIIC4 from Haemophilus parainfluenzae
Summary for 7MSL
| Entry DOI | 10.2210/pdb7msl/pdb |
| Descriptor | AcrIIC4, IODIDE ION (3 entities in total) |
| Functional Keywords | anti-crispr proteins, acriic4, a haemophilus parainfluenzae prophage, viral protein |
| Biological source | Haemophilus parainfluenzae |
| Total number of polymer chains | 1 |
| Total formula weight | 10712.43 |
| Authors | Pan, C.,Maxwell, K.L.,Moraes, T.F. (deposition date: 2021-05-11, release date: 2022-03-23, Last modification date: 2024-05-22) |
| Primary citation | Hwang, S.,Pan, C.,Garcia, B.,Davidson, A.R.,Moraes, T.F.,Maxwell, K.L. Structural and Mechanistic Insight into CRISPR-Cas9 Inhibition by Anti-CRISPR Protein AcrIIC4 Hpa. J.Mol.Biol., 434:167420-167420, 2022 Cited by PubMed Abstract: 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 AcrIIC4 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. AcrIIC4 likely acts by blocking the conformational changes that allow the HNH and RuvC endonuclease domains to contact the DNA sites to be nicked. PubMed: 34954237DOI: 10.1016/j.jmb.2021.167420 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.73 Å) |
Structure validation
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