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Crystal structure of the arginine repressor protein from Mycobacterium tuberculosis in complex with the DNA operatorCrystal structure of the arginine repressor protein from Mycobacterium tuberculosis in complex with the DNA operator
Structural highlights
FunctionARGR_MYCTU Regulates arginine biosynthesis genes (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. See AlsoReferences
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