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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Sep 1;66(Pt 9):1060-3. doi: 10.1107/S1744309110028617. Epub 2010 Aug 26.

Preliminary crystallographic analysis of the Escherichia coli antitoxin MqsA (YgiT/b3021) in complex with mqsRA promoter DNA.

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Department of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Box G-E3, Providence, RI 02912, USA.


The Escherichia coli proteins MqsR and MqsA comprise a novel toxin-antitoxin (TA) system. MqsA, the antitoxin, defines a new family of antitoxins because unlike other antitoxins MqsA is structured throughout its entire sequence, binds zinc and coordinates DNA via its C-terminal and not its N-terminal domain. In order to understand how bacterial antitoxins, and MqsA in particular, regulate transcription, the MqsA protein was cocrystallized with a 26-mer duplex DNA corresponding to the palindromic region of the mqsRA promoter. The merohedrally twinned crystal belonged to space group P4(1), with unit-cell parameters a=60.99, b=60.99, c=148.60 A. A complete data set was collected to a resolution of 2.1 A. The solvent content of the crystal was consistent with the presence of two MqsA molecules bound to the duplex DNA in the asymmetric unit.

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