Structural highlights
Publication Abstract from PubMed
The Hha and TomB proteins from Escherichia coli form an oxygen-dependent toxin-antitoxin (TA) system. Here we show that YmoB, the Yersinia orthologue of TomB, and its single cysteine variant [C117S]YmoB can replace TomB as antitoxins in E. coli. In contrast to other TA systems, [C117S]YmoB transiently interacts with Hha (rather than forming a stable complex) and enhances the spontaneous oxidation of the Hha conserved cysteine residue to a -SOxH-containing species (sulfenic, sulfinic or sulfonic acid), which destabilizes the toxin. The nuclear magnetic resonance structure of [C117S]YmoB and the homology model of TomB show that the two proteins form a four-helix bundle with a conserved buried cysteine connected to the exterior by a channel with a diameter comparable to that of an oxygen molecule. The Hha interaction site is located on the opposite side of the helix bundle.
An oxygen-sensitive toxin-antitoxin system.,Marimon O, Teixeira JM, Cordeiro TN, Soo VW, Wood TL, Mayzel M, Amata I, Garcia J, Morera A, Gay M, Vilaseca M, Orekhov VY, Wood TK, Pons M Nat Commun. 2016 Dec 8;7:13634. doi: 10.1038/ncomms13634. PMID:27929062[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Marimon O, Teixeira JM, Cordeiro TN, Soo VW, Wood TL, Mayzel M, Amata I, Garcia J, Morera A, Gay M, Vilaseca M, Orekhov VY, Wood TK, Pons M. An oxygen-sensitive toxin-antitoxin system. Nat Commun. 2016 Dec 8;7:13634. doi: 10.1038/ncomms13634. PMID:27929062 doi:http://dx.doi.org/10.1038/ncomms13634
