1H, 13C, and 15N backbone and side chain chemical shift assignment of YdaS, a monomeric member of the HigA family

Maruša Prolič Kalinšek, Pieter De Bruyn, Dukas Jurenas, Laurence Van Melderen, Remy Loris, Oleksandr Volkov

Research output: Contribution to journalArticle

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 1H, 15N and 13C 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.
Original languageEnglish
Pages (from-to)25-30
Number of pages6
JournalBiomolecular NMR Assignments
Volume14
Issue number1
DOIs
Publication statusPublished - Apr 2020

Keywords

  • NMR spectroscopy
  • protein structure
  • Structural biology
  • Toxin-antitoxin module

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