8phj | pdb_00008phj

cA4-bound Cami1 in complex with 70S ribosome

spinqualitylabelsall models 8phj, resolution 3.67Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8phj is a 11 chain structure with sequence from Escherichia coli and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.67Å Ligands: 1MG, 2MA, 2MG, 3TD, 4OC, 4SU, 5MC, 5MU, 6MZ, A2M, G7M, H2U, IAS, MA6, MEQ, MG, OMC, OMG, OMU, PSU, UR3, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RL33_ECOLI Publication Abstract from PubMed Prokaryotic type III CRISPR-Cas antiviral systems employ cyclic oligoadenylate (cA(n)) signaling to activate a diverse range of auxiliary proteins that reinforce the CRISPR-Cas defense. Here we characterize a class of cA(n)-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(4)), 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(4) 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. Ribosomal stalk-captured CARF-RelE ribonuclease inhibits translation following CRISPR signaling.,Mogila I, Tamulaitiene G, Keda K, Timinskas A, Ruksenaite A, Sasnauskas G, Venclovas C, Siksnys V, Tamulaitis G Science. 2023 Dec;382(6674):1036-1041. doi: 10.1126/science.adj2107. Epub 2023 , Nov 30. PMID:38033086 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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