| Literature DB >> 31625047 |
Maruša Prolič-Kalinšek1,2, Pieter De Bruyn1,2, Dukas Jurėnas3, Laurence Van Melderen3, Remy Loris4,5, Alexander N Volkov1,2,6.
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.Entities:
Keywords: DNA binding; Macromolecular structure; Toxin–antitoxin module; Transcription regulation
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Year: 2019 PMID： 31625047 DOI： 10.1007/s12104-019-09915-9
Source DB: PubMed Journal: Biomol NMR Assign ISSN： 1874-270X Impact factor: 0.746