|Title||H, C, and N backbone and side chain chemical shift assignment of YdaS, a monomeric member of the HigA family.|
|Publication Type||Journal Article|
|Year of Publication||2019|
|Authors||Prolič-Kalinšek, M., P. De Bruyn, D. Jurenas, L. Van Melderen, R. Loris, and A. N. Volkov|
|Journal||Biomol NMR Assign|
|Date Published||2019 Oct 17|
The cryptic prophage CP-933P in Escherichia coli O157:H7 contains a parDE-like toxin-antitoxin module, the operator region of which is recognized by two flanking transcription regulators: PaaR2 (ParE associated Regulator), which forms part of the paaR2-paaA2-parE2 toxin-antitoxin operon and YdaS (COG4197), which is encoded in the opposite direction but shares the operator. Here we report the H, N and C backbone and side chain chemical shift assignments of YdaS from Escherichia coli O157:H7 in its free state. YdaS is a distinct relative to HigA antitoxins but behaves as a monomer in solution. The BMRB Accession Number is 27917.
|Alternate Journal||Biomol NMR Assign|
|Grant List||G.0226.17N / / Fonds Wetenschappelijk Onderzoek / |
SPR13 / / Vrije Universiteit Brussel /
H, C, and N backbone and side chain chemical shift assignment of YdaS, a monomeric member of the HigA family.