6Q1H

Structure of P. aeruginosa ATCC27853 NucC, cAAA-bound form

Summary for 6Q1H

• Entry DOI: 10.2210/pdb6q1h/pdb
• Related: 6P7O 6P7P 6P7Q
• Descriptor: Bacterial protein ORF C62, RNA (5'-R(P*AP*AP*A)-3') (3 entities in total)
• Functional Keywords: nuclease, dna binding protein, dna binding protein-rna complex, dna binding protein/rna
• Biological source: Pseudomonas aeruginosa; More
• Total number of polymer chains: 8
• Total formula weight: 162014.20

Authors

Ye, Q.,Lau, R.K.,Corbett, K.D. (deposition date: 2019-08-04, release date: 2019-12-25, Last modification date: 2023-10-11)

Primary citation

Lau, R.K.,Ye, Q.,Birkholz, E.A.,Berg, K.R.,Patel, L.,Mathews, I.T.,Watrous, J.D.,Ego, K.,Whiteley, A.T.,Lowey, B.,Mekalanos, J.J.,Kranzusch, P.J.,Jain, M.,Pogliano, J.,Corbett, K.D.
Structure and Mechanism of a Cyclic Trinucleotide-Activated Bacterial Endonuclease Mediating Bacteriophage Immunity.
Mol.Cell, 77:723-, 2020

PubMed Abstract: Bacteria possess an array of defenses against foreign invaders, including a broadly distributed bacteriophage defense system termed CBASS (cyclic oligonucleotide-based anti-phage signaling system). In CBASS systems, a cGAS/DncV-like nucleotidyltransferase synthesizes cyclic di- or tri-nucleotide second messengers in response to infection, and these molecules activate diverse effectors to mediate bacteriophage immunity via abortive infection. Here, we show that the CBASS effector NucC is related to restriction enzymes but uniquely assembles into a homotrimer. Binding of NucC trimers to a cyclic tri-adenylate second messenger promotes assembly of a NucC homohexamer competent for non-specific double-strand DNA cleavage. In infected cells, NucC activation leads to complete destruction of the bacterial chromosome, causing cell death prior to completion of phage replication. In addition to CBASS systems, we identify NucC homologs in over 30 type III CRISPR/Cas systems, where they likely function as accessory nucleases activated by cyclic oligoadenylate second messengers synthesized by these systems' effector complexes.

PubMed: 31932164
DOI: 10.1016/j.molcel.2019.12.010

Experimental method

X-RAY DIFFRACTION (1.45 Å)