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2XDD

A processed non-coding RNA regulates a bacterial antiviral system

Summary for 2XDD
Entry DOI10.2210/pdb2xdd/pdb
Related2XD0 2XDB
DescriptorTOXN, TOXI, ZINC ION, ... (4 entities in total)
Functional Keywordstoxin-rna complex, abortive infection, phage, toxin, toxin/rna
Biological sourcePECTOBACTERIUM ATROSEPTICUM
More
Total number of polymer chains6
Total formula weight95395.32
Authors
Blower, T.R.,Pei, X.Y.,Short, F.L.,Fineran, P.C.,Humphreys, D.P.,Luisi, B.F.,Salmond, G.P.C. (deposition date: 2010-04-30, release date: 2011-01-12, Last modification date: 2024-11-06)
Primary citationFineran, P.C.,Blower, T.R.,Foulds, I.J.,Humphreys, D.P.,Lilley, K.S.,Salmond, G.P.C.
The Phage Abortive Infection System, Toxin, Functions as a Protein-RNA Toxin-Antitoxin Pair.
Proc.Natl.Acad.Sci.USA, 106:894-, 2009
Cited by
PubMed Abstract: Various mechanisms exist that enable bacteria to resist bacteriophage infection. Resistance strategies include the abortive infection (Abi) systems, which promote cell death and limit phage replication within a bacterial population. A highly effective 2-gene Abi system from the phytopathogen Erwinia carotovora subspecies atroseptica, designated ToxIN, is described. The ToxIN Abi system also functions as a toxin-antitoxin (TA) pair, with ToxN inhibiting bacterial growth and the tandemly repeated ToxI RNA antitoxin counteracting the toxicity. TA modules are currently divided into 2 classes, protein and RNA antisense. We provide evidence that ToxIN defines an entirely new TA class that functions via a novel protein-RNA mechanism, with analogous systems present in diverse bacteria. Despite the debated role of TA systems, we demonstrate that ToxIN provides viral resistance in a range of bacterial genera against multiple phages. This is the first demonstration of a novel mechanistic class of TA systems and of an Abi system functioning in different bacterial genera, both with implications for the dynamics of phage-bacterial interactions.
PubMed: 19124776
DOI: 10.1073/PNAS.0808832106
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.2 Å)
Structure validation

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