# metadata.dc.description.abstract[].value
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.

# metadata.dc.relation.ispartof[].value
Nature Communications, 2016, vol. 7, num. 13634

# metadata.dc.rights[].value
cc-by (c) Marimon Garrido, Oriol et al., 2016

# metadata.dc.source[].value
Articles publicats en revistes (Química Inorgànica i Orgànica)

# metadata.dc.subject.classification[].value
Espectroscòpia de ressonància magnètica nuclear