2MN2

3D structure of YmoB, a modulator of biofilm formation

Summary for 2MN2

• Entry DOI: 10.2210/pdb2mn2/pdb
• NMR Information: BMRB: 19876
• Descriptor: YmoB (1 entity in total)
• Functional Keywords: four helix bundle, buried cysteine, antitoxin
• Biological source: Yersinia enterocolitica
• Total number of polymer chains: 1
• Total formula weight: 15514.28

Authors

Marimon, O.,Cordeiro, T.N.,Amata, I.,Pons, M. (deposition date: 2014-03-26, release date: 2015-04-01, Last modification date: 2024-05-15)

Primary citation

Marimon, O.,Teixeira, J.M.,Cordeiro, T.N.,Soo, V.W.,Wood, T.L.,Mayzel, M.,Amata, I.,Garcia, J.,Morera, A.,Gay, M.,Vilaseca, M.,Orekhov, V.Y.,Wood, T.K.,Pons, M.
An oxygen-sensitive toxin-antitoxin system.
Nat Commun, 7:13634-13634, 2016

PubMed Abstract: 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 -SOH-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.

PubMed: 27929062
DOI: 10.1038/ncomms13634

Experimental method

SOLUTION NMR