8PHJ

cA4-bound Cami1 in complex with 70S ribosome

This is a non-PDB format compatible entry.

Summary for 8PHJ

• Entry DOI: 10.2210/pdb8phj/pdb
• Related: 8PHB
• EMDB information: 17663 17664 17665 17666 17667
• Related PRD ID: PRD_002431
• Descriptor: Large ribosomal subunit protein bL33, 16S rRNA, Small ribosomal subunit protein uS2, ... (61 entities in total)
• Functional Keywords: crispr, cyclic oligoadenylate, rnase, rele-toxin, hydrolase, ribosome
• Biological source: Allochromatium vinosum; More
• Total number of polymer chains: 61
• Total formula weight: 2344052.72

Authors

Tamulaitiene, G.,Mogila, I.,Sasnauskas, G.,Tamulaitis, G. (deposition date: 2023-06-20, release date: 2023-12-13, Last modification date: 2024-04-24)

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

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: 38033086
DOI: 10.1126/science.adj2107

Experimental method

ELECTRON MICROSCOPY (3.67 Å)