4GLK
Structure and activity of AbiQ, a lactococcal anti-phage endoribonuclease belonging to the type-III toxin-antitoxin system
Summary for 4GLK
| Entry DOI | 10.2210/pdb4glk/pdb |
| Descriptor | AbiQ, GLYCEROL (3 entities in total) |
| Functional Keywords | alpha beta, endonuclease, rna antiq, hydrolase |
| Biological source | Lactococcus lactis |
| Total number of polymer chains | 1 |
| Total formula weight | 20585.01 |
| Authors | Samson, J.,Spinelli, S.,Cambillau, C.,Moineau, S. (deposition date: 2012-08-14, release date: 2013-01-16, Last modification date: 2023-09-13) |
| Primary citation | Samson, J.E.,Spinelli, S.,Cambillau, C.,Moineau, S. Structure and activity of AbiQ, a lactococcal endoribonuclease belonging to the type III toxin-antitoxin system. Mol.Microbiol., 87:756-768, 2013 Cited by PubMed Abstract: AbiQ is a phage resistance mechanism found on a native plasmid of Lactococcus lactis that abort virulent phage infections. In this study, we experimentally demonstrate that AbiQ belongs to the recently described type III toxin-antitoxin systems. When overexpressed, the AbiQ protein (ABIQ) is toxic and causes bacterial death in a bacteriostatic manner. Northern and Western blot experiments revealed that the abiQ gene is transcribed and translated constitutively, and its expression is not activated by a phage product. ABIQ is an endoribonuclease that specifically cleaves its cognate antitoxin RNA molecule in vivo. The crystal structure of ABIQ was solved and site-directed mutagenesis identified key amino acids for its anti-phage and/or its RNase function. The AbiQ system is the first lactococcal abortive infection system characterized to date at a structural level. PubMed: 23279123DOI: 10.1111/mmi.12129 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.16 Å) |
Structure validation
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