6U7B
Structure of E. coli MS115-1 CdnC:HORMA-deltaN complex
Summary for 6U7B
| Entry DOI | 10.2210/pdb6u7b/pdb |
| Descriptor | E. coli MS115-1 CdnC, bacHORMA_1 domain-containing protein, MAGNESIUM ION, ... (7 entities in total) |
| Functional Keywords | second-messenger signaling, cgas, cd-ntase, horma domain, closure motif, signaling protein |
| Biological source | Escherichia coli MS 115-1 More |
| Total number of polymer chains | 4 |
| Total formula weight | 113492.79 |
| Authors | Ye, Q.,Corbett, K.D. (deposition date: 2019-09-02, release date: 2019-12-25, Last modification date: 2023-10-11) |
| Primary citation | Ye, Q.,Lau, R.K.,Mathews, I.T.,Birkholz, E.A.,Watrous, J.D.,Azimi, C.S.,Pogliano, J.,Jain, M.,Corbett, K.D. HORMA Domain Proteins and a Trip13-like ATPase Regulate Bacterial cGAS-like Enzymes to Mediate Bacteriophage Immunity. Mol.Cell, 77:709-, 2020 Cited by PubMed Abstract: Bacteria are continually challenged by foreign invaders, including bacteriophages, and have evolved a variety of defenses against these invaders. Here, we describe the structural and biochemical mechanisms of a bacteriophage immunity pathway found in a broad array of bacteria, including E. coli and Pseudomonas aeruginosa. This pathway uses eukaryotic-like HORMA domain proteins that recognize specific peptides, then bind and activate a cGAS/DncV-like nucleotidyltransferase (CD-NTase) to generate a cyclic triadenylate (cAAA) second messenger; cAAA in turn activates an endonuclease effector, NucC. Signaling is attenuated by a homolog of the AAA+ ATPase Pch2/TRIP13, which binds and disassembles the active HORMA-CD-NTase complex. When expressed in non-pathogenic E. coli, this pathway confers immunity against bacteriophage λ through an abortive infection mechanism. Our findings reveal the molecular mechanisms of a bacterial defense pathway integrating a cGAS-like nucleotidyltransferase with HORMA domain proteins for threat sensing through protein detection and negative regulation by a Trip13 ATPase. PubMed: 31932165DOI: 10.1016/j.molcel.2019.12.009 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.09 Å) |
Structure validation
Download full validation report
