EMD-17664

Single-particle
3.63 Å
EMD-17664 Deposition: 20/06/2023
Map released: 13/12/2023
Last modified: 27/03/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-17664

Cami1-ribosome local refinement map with mask on Cami1 and L12-Cter

EMD-17664

Single-particle
3.63 Å
EMD-17664 Deposition: 20/06/2023
Map released: 13/12/2023
Last modified: 27/03/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Escherichia coli
Sample: Cami1 bound in 70S E.coli ribosome

Deposition Authors: Tamulaitiene G , Mogila I , Sasnauskas G , Tamulaitis G
Ribosomal stalk-captured CARF-RelE ribonuclease inhibits translation following CRISPR signaling.
PUBMED: 38033086
DOI: doi:10.1126/science.adj2107
ISSN: 1095-9203
ASTM: SCIEAS
Abstract:
Prokaryotic type III CRISPR-Cas antiviral systems employ cyclic oligoadenylate (cAn) signaling to activate a diverse range of auxiliary proteins that reinforce the CRISPR-Cas defense. Here we characterize a class of cAn-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 (cA4), 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-cA4 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.