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Publication Abstract from PubMed

The arginine repressor (ArgR) from Mycobacterium tuberculosis (Mtb) is a gene product encoded by the open reading frame Rv1657. It regulates the L-arginine concentration in cells by interacting with ARG boxes in the promoter regions of the arginine biosynthesis and catabolism operons. Here we present a 2.5-A structure of MtbArgR in complex with a 16-bp DNA operator in the absence of arginine. A biological trimer of the protein-DNA complex is formed via the crystallographic 3-fold symmetry axis. The N-terminal domain of MtbArgR has a winged helix-turn-helix motif that binds to the major groove of the DNA. This structure shows that, in the absence of arginine, the ArgR trimer can bind three ARG box half-sites. It also reveals the structure of the whole MtbArgR molecule itself containing both N-terminal and C-terminal domains.

Crystal structure of the arginine repressor protein in complex with the DNA operator from Mycobacterium tuberculosis.,Cherney LT, Cherney MM, Garen CR, Lu GJ, James MN J Mol Biol. 2008 Dec 31;384(5):1330-40. Epub 2008 Oct 15. PMID:18952097^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.