8f3k

Anti-CRISPR protein AcrIIC5 inhibits CRISPR-Cas9 by acting as a DNA mimic

spinqualitylabelsall models 8f3k, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8f3k is a 1 chain structure with sequence from Neisseria chenwenguii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: GOL, MSE, NH4, TRS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A220S190_9NEIS Publication Abstract from PubMed Anti-CRISPR proteins inhibit CRISPR-Cas immune systems through diverse mechanisms. Previously, the anti-CRISPR protein AcrIIC5(Smu) was shown to potently inhibit a type II-C Cas9 from Neisseria meningitidis (Nme1Cas9). In this work, we explore the mechanism of activity of the AcrIIC5 homologue from Neisseria chenwenguii (AcrIIC5(Nch)) and show that it prevents Cas9 binding to target DNA. We show that AcrIIC5(Nch) targets the PAM-interacting domain (PID) of Nme1Cas9 for inhibition, agreeing with previous findings for AcrIIC5(Smu), and newly establish that strong binding of the anti-CRISPR requires guide RNA be pre-loaded on Cas9. We determined the crystal structure of AcrIIC5(Nch) using X-ray crystallography and identified amino acid residues that are critical for its function. Using a protein docking algorithm we show that AcrIIC5(Nch) likely occupies the Cas9 DNA binding pocket, thereby inhibiting target DNA binding through a mechanism similar to that previously described for AcrIIA2 and AcrIIA4. Anti-CRISPR Protein AcrIIC5 Inhibits CRISPR-Cas9 by Occupying the Target DNA Binding Pocket.,Hwang S, Shah M, Garcia B, Hashem N, Davidson AR, Moraes TF, Maxwell KL J Mol Biol. 2023 Apr 1;435(7):167991. doi: 10.1016/j.jmb.2023.167991. Epub 2023 , Feb 2. PMID:36736884 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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