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 |
ISSN | 1874-270X |
Abstract | 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. |
DOI | 10.1007/s12104-019-09915-9 |
Alternate Journal | Biomol NMR Assign |
PubMed ID | 31625047 |
Grant List | G.0226.17N / / Fonds Wetenschappelijk Onderzoek / SPR13 / / Vrije Universiteit Brussel / |
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