Function

Arginine repressor (ArgR) is a prokaryotic repressor which regulates the arginine deiminase pathway. In this pathway, arginine is metabolized to form ammonia, CO2 and ATP. The ArgR releases the expression of the arginine deiminase pathway in the presence of arginine. The genes controlled by ArgR are not found in a single operon. While repressors are usually active as dimers, ArgR is a hexamer and binds to 2 palindromic DNA sites called ARG box in its N terminal domain.[1]

Structural highlights

The structure of ArgR shows a DNA-binding domain at the acidic N-terminal and a basic C-terminal domain which contains the and the . Every Arg ligand interacts .[2]

3D structures of arginine repressor

Arginine repressor 3D structures


E. coli structure of arginine repressor C terminal hexamer complex with arginine (PDB entry 1xxb)

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ReferencesReferences

  1. Ni J, Sakanyan V, Charlier D, Glansdorff N, Van Duyne GD. Structure of the arginine repressor from Bacillus stearothermophilus. Nat Struct Biol. 1999 May;6(5):427-32. PMID:10331868 doi:http://dx.doi.org/10.1038/8229
  2. Van Duyne GD, Ghosh G, Maas WK, Sigler PB. Structure of the oligomerization and L-arginine binding domain of the arginine repressor of Escherichia coli. J Mol Biol. 1996 Feb 23;256(2):377-91. PMID:8594204 doi:http://dx.doi.org/10.1006/jmbi.1996.0093

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