Preliminary Crystallographic Analysis of the Escherichia coli Antitoxin MqsA (YgiT/b3021) in Complex with mqsRA Promoter DNA
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{sub 1}, with unit-cell parameters a = 60.99, b = 60.99, c = 148.60 {angstrom}. A complete data set was collected to a resolution of 2.1 {angstrom}. The solvent content of the crystal was consistent with the presence of two MqsA molecules bound to the duplex DNA in the asymmetric unit.
- Research Organization:
- Brookhaven National Lab. (BNL), Upton, NY (United States). National Synchrotron Light Source
- Sponsoring Organization:
- DOE - OFFICE OF SCIENCE
- DOE Contract Number:
- DE-AC02-98CH10886
- OSTI ID:
- 1020107
- Report Number(s):
- BNL-95956-2011-JA; TRN: US201116%%88
- Journal Information:
- Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 66, Issue 9; ISSN 1744-3091
- Country of Publication:
- United States
- Language:
- English
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