7XI5
Anti-CRISPR-associated Aca10
Summary for 7XI5
| Entry DOI | 10.2210/pdb7xi5/pdb |
| Descriptor | Transcriptional regulator (2 entities in total) |
| Functional Keywords | aca10, immune system, dna binding protein, autoregulator |
| Biological source | Pseudomonas citronellolis |
| Total number of polymer chains | 4 |
| Total formula weight | 28432.32 |
| Authors | Lee, S.Y.,Park, H.H. (deposition date: 2022-04-12, release date: 2023-02-22, Last modification date: 2023-11-29) |
| Primary citation | Lee, S.Y.,Birkholz, N.,Fineran, P.C.,Park, H.H. Molecular basis of anti-CRISPR operon repression by Aca10. Nucleic Acids Res., 50:8919-8928, 2022 Cited by PubMed Abstract: CRISPR-Cas systems are bacterial defense systems for fighting against invaders such as bacteriophages and mobile genetic elements. To escape destruction by these bacterial immune systems, phages have co-evolved multiple anti-CRISPR (Acr) proteins, which inhibit CRISPR-Cas function. Many acr genes form an operon with genes encoding transcriptional regulators, called anti-CRISPR-associated (Aca) proteins. Aca10 is the most recently discovered Aca family that is encoded within an operon containing acrIC7 and acrIC6 in Pseudomonas citronellolis. Here, we report the high-resolution crystal structure of an Aca10 protein to unveil the molecular basis of transcriptional repressor role of Aca10 in the acrIC7-acrIC6-aca10 operon. We identified that Aca10 forms a dimer in solution, which is critical for binding specific DNA. We also showed that Aca10 directly recognizes a 21 bp palindromic sequence in the promoter of the acr operon. Finally, we revealed that R44 of Aca10 is a critical residue involved in the DNA binding, which likely results in a high degree of DNA bending. PubMed: 35920325DOI: 10.1093/nar/gkac656 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.76 Å) |
Structure validation
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