Arginine repressor ArgR

In molecular biology, the arginine repressor (ArgR) is a repressor of prokaryotic arginine deiminase pathways.

Arginine repressor, C-terminal domain
c-terminal domain of escherichia coli arginine repressor/ l-arginine complex; pb derivative
Identifiers
Symbol	Arg_repressor_C
Pfam	PF02863
InterPro	IPR020899
SCOP2	1aoy / SCOPe / SUPFAM
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Arginine repressor, DNA binding domain
Identifiers
Symbol	Arg_repressor
Pfam	PF01316
SCOP2	1aoy / SCOPe / SUPFAM
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

The arginine dihydrolase (AD) pathway is found in many prokaryotes and some eukaryotes, an example of the latter being Giardia lamblia (Giardia intestinalis).^[1] The three-enzyme anaerobic pathway breaks down L-arginine to form 1 mol of ATP, carbon dioxide and ammonia. In some bacteria, the first enzyme, arginine deiminase, can account for up to 10% of total cell protein.^[1]

Most prokaryotic arginine deiminase pathways are under the control of a repressor gene, termed ArgR.^[2] This is a negative regulator, and will only release the arginine deiminase operon for expression in the presence of arginine.^[3] The crystal structure of apo-ArgR from Bacillus stearothermophilus has been determined to 2.5A by means of X-ray crystallography.^[4] The protein exists as a hexamer of identical subunits, and is shown to have six DNA-binding domains, clustered around a central oligomeric core when bound to arginine. It predominantly interacts with A.T residues in ARG boxes. This hexameric protein binds DNA at its N terminus to repress arginine biosynthesis or activate arginine catabolism. Some species have several ArgR paralogs. In a neighbour-joining tree, some of these paralogous sequences show long branches and differ significantly from the well-conserved C-terminal region.