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6P7O

Structure of E. coli MS115-1 NucC, Apo form

Summary for 6P7O
Entry DOI10.2210/pdb6p7o/pdb
DescriptorE. coli MS115-1 NucC, MAGNESIUM ION, HEXAETHYLENE GLYCOL, ... (6 entities in total)
Functional Keywordsnuclease, dna binding protein
Biological sourceEscherichia coli MS 115-1
Total number of polymer chains1
Total formula weight27248.56
Authors
Ye, Q.,Lau, R.K.,Berg, K.R.,Corbett, K.D. (deposition date: 2019-06-06, release date: 2019-12-25, Last modification date: 2024-03-13)
Primary citationLau, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.752 Å)
Structure validation

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