title: Preliminary crystallographic analysis of the Escherichia coli antitoxin MqsA (YgiT/b3021) in complex with mqsRA promoter DNA.
abstract: 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.
authors.affiliation: Department of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Box G-E3, Providence, RI 02912, USA.
authors.forename: Breann L
authors.initials: BL
authors.lastname: Brown
authors.forename: Rebecca
authors.initials: R
authors.lastname: Page
mesh_terms: D018360:Crystallography, X-Ray; D004269:DNA, Bacterial / Q000737:chemistry* / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry*; D004926:Escherichia coli / Q000737:chemistry*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism; D011401:Promoter Regions, Genetic; D011485:Protein Binding
chemical_list: D004269:DNA, Bacterial; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; C555039:MqsA protein, E coli; C508571:MqsR protein, E coli
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