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8B0R

Structure of the CalpL/cA4 complex

Summary for 8B0R
Entry DOI10.2210/pdb8b0r/pdb
Related7QDA 8B0U
Related PRD IDPRD_002431
DescriptorSMODS-associated and fused to various effectors domain-containing protein, Cyclic tetraadenosine monophosphate (cA4), TRIETHYLENE GLYCOL, ... (5 entities in total)
Functional Keywordsprotease, crispr type iii, coa, ca4, peptide binding protein, hydrolase
Biological sourceSulfurihydrogenibium
More
Total number of polymer chains2
Total formula weight59807.20
Authors
Schneberger, N.,Hagelueken, G. (deposition date: 2022-09-08, release date: 2022-11-16, Last modification date: 2024-02-07)
Primary citationRouillon, C.,Schneberger, N.,Chi, H.,Blumenstock, K.,Da Vela, S.,Ackermann, K.,Moecking, J.,Peter, M.F.,Boenigk, W.,Seifert, R.,Bode, B.E.,Schmid-Burgk, J.L.,Svergun, D.,Geyer, M.,White, M.F.,Hagelueken, G.
Antiviral signalling by a cyclic nucleotide activated CRISPR protease.
Nature, 614:168-174, 2023
Cited by
PubMed Abstract: CRISPR defence systems such as the well-known DNA-targeting Cas9 and the RNA-targeting type III systems are widespread in prokaryotes. The latter orchestrates a complex antiviral response that is initiated through the synthesis of cyclic oligoadenylates after recognition of foreign RNA. Among the large set of proteins that are linked to type III systems and predicted to bind cyclic oligoadenylates, a CRISPR-associated Lon protease (CalpL) stood out to us. CalpL contains a sensor domain of the SAVED family fused to a Lon protease effector domain. However, the mode of action of this effector is unknown. Here we report the structure and function of CalpL and show that this soluble protein forms a stable tripartite complex with two other proteins, CalpT and CalpS, that are encoded on the same operon. After activation by cyclic tetra-adenylate (cA), CalpL oligomerizes and specifically cleaves the MazF homologue CalpT, which releases the extracytoplasmic function σ factor CalpS from the complex. Our data provide a direct connection between CRISPR-based detection of foreign nucleic acids and transcriptional regulation. Furthermore, the presence of a SAVED domain that binds cyclic tetra-adenylate in a CRISPR effector reveals a link to the cyclic-oligonucleotide-based antiphage signalling system.
PubMed: 36423657
DOI: 10.1038/s41586-022-05571-7
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

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