2P5M

C-terminal domain hexamer of AhrC bound with L-arginine

Summary for 2P5M

• Entry DOI: 10.2210/pdb2p5m/pdb
• Related: 2P5K 2P5L
• Descriptor: Arginine repressor, ARGININE (3 entities in total)
• Functional Keywords: alpha-beta, l-arginine binding domain, dna binding protein
• Biological source: Bacillus subtilis
• Cellular location: Cytoplasm: P17893
• Total number of polymer chains: 3
• Total formula weight: 28745.84

Authors

Garnett, J.A.,Baumberg, S.,Stockley, P.G.,Phillips, S.E.V. (deposition date: 2007-03-15, release date: 2007-10-30, Last modification date: 2023-08-30)

Primary citation

Garnett, J.A.,Baumberg, S.,Stockley, P.G.,Phillips, S.E.
Structure of the C-terminal effector-binding domain of AhrC bound to its corepressor L-arginine.
Acta Crystallogr.,Sect.F, 63:918-921, 2007

PubMed Abstract: The arginine repressor/activator protein (AhrC) from Bacillus subtilis belongs to a large family of multifunctional transcription factors that are involved in the regulation of bacterial arginine metabolism. AhrC interacts with operator sites in the promoters of arginine biosynthetic and catabolic operons, acting as a transcriptional repressor at biosynthetic sites and an activator of transcription at catabolic sites. AhrC is a hexamer of identical subunits, each having two domains. The C-terminal domains form the core of the protein and are involved in oligomerization and L-arginine binding. The N-terminal domains lie on the outside of the compact core and play a role in binding to 18 bp DNA operators called ARG boxes. The C-terminal domain of AhrC has been expressed, purified and characterized, and also crystallized as a hexamer with the bound corepressor L-arginine. Here, the crystal structure refined to 1.95 A is presented.

PubMed: 18007040
DOI: 10.1107/S1744309107049391

Experimental method

X-RAY DIFFRACTION (1.95 Å)