3ERE

Crystal structure of the arginine repressor protein from Mycobacterium tuberculosis in complex with the DNA operator

Summary for 3ERE

• Entry DOI: 10.2210/pdb3ere/pdb
• Related: 2ZFZ 3BUE 3CAG
• Descriptor: Arginine repressor, 5'-D(*DTP*DTP*DGP*DCP*DAP*DTP*DAP*DAP*DCP*DGP*DAP*DTP*DGP*DCP*DAP*DA)-3', 5'-D(*DTP*DTP*DGP*DCP*DAP*DTP*DCP*DGP*DTP*DTP*DAP*DTP*DGP*DCP*DAP*DA)-3', ... (5 entities in total)
• Functional Keywords: mycobacterium tuberculosis, arginine repressor protein, dna binding, argr-operator complex, structural genomics, tb structural genomics, tb structural genomics consortium, tbsgc, amino-acid biosynthesis, arginine biosynthesis, dna-binding, transcription, transcription regulation, dna binding protein-dna complex, dna binding protein/dna
• Biological source: Mycobacterium tuberculosis; More
• Cellular location: Cytoplasm (Probable): P0A4Y8
• Total number of polymer chains: 3
• Total formula weight: 27449.23

Authors

Cherney, L.T.,Cherney, M.M.,Garen, C.R.,Lu, G.J.,James, M.N.,TB Structural Genomics Consortium (TBSGC) (deposition date: 2008-10-01, release date: 2008-10-14, Last modification date: 2023-09-06)

Primary citation

Cherney, L.T.,Cherney, M.M.,Garen, C.R.,Lu, G.J.,James, M.N.
Crystal structure of the arginine repressor protein in complex with the DNA operator from Mycobacterium tuberculosis.
J.Mol.Biol., 384:1330-1340, 2008

PubMed Abstract: 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.

PubMed: 18952097
DOI: 10.1016/j.jmb.2008.10.015

Experimental method

X-RAY DIFFRACTION (2.5 Å)