8PHB
Crystal structure of apo Cami1
Summary for 8PHB
| Entry DOI | 10.2210/pdb8phb/pdb |
| Descriptor | CRISPR-associated protein, APE2256 family (2 entities in total) |
| Functional Keywords | crispr, cyclic oligoadenylate, rnase, rele-toxin, hydrolase |
| Biological source | Allochromatium vinosum |
| Total number of polymer chains | 2 |
| Total formula weight | 91808.23 |
| Authors | Tamulaitiene, G.,Tamulaitis, G.,Mogila, I.,Keda, K. (deposition date: 2023-06-19, release date: 2023-12-13, Last modification date: 2024-03-27) |
| Primary citation | Mogila, I.,Tamulaitiene, G.,Keda, K.,Timinskas, A.,Ruksenaite, A.,Sasnauskas, G.,Venclovas, C.,Siksnys, V.,Tamulaitis, G. Ribosomal stalk-captured CARF-RelE ribonuclease inhibits translation following CRISPR signaling. Science, 382:1036-1041, 2023 Cited by PubMed Abstract: Prokaryotic type III CRISPR-Cas antiviral systems employ cyclic oligoadenylate (cA) signaling to activate a diverse range of auxiliary proteins that reinforce the CRISPR-Cas defense. Here we characterize a class of cA-dependent effector proteins named CRISPR-Cas-associated messenger RNA (mRNA) interferase 1 (Cami1) consisting of a CRISPR-associated Rossmann fold sensor domain fused to winged helix-turn-helix and a RelE-family mRNA interferase domain. Upon activation by cyclic tetra-adenylate (cA), Cami1 cleaves mRNA exposed at the ribosomal A-site thereby depleting mRNA and leading to cell growth arrest. The structures of apo-Cami1 and the ribosome-bound Cami1-cA complex delineate the conformational changes that lead to Cami1 activation and the mechanism of Cami1 binding to a bacterial ribosome, revealing unexpected parallels with eukaryotic ribosome-inactivating proteins. PubMed: 38033086DOI: 10.1126/science.adj2107 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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