2P5K

Crystal structure of the N-terminal domain of AhrC

Summary for 2P5K

• Entry DOI: 10.2210/pdb2p5k/pdb
• Related: 2P5L 2P5M
• Descriptor: Arginine repressor (2 entities in total)
• Functional Keywords: dna-binding domain, winged helix-turn-helix (whth), dna binding protein
• Biological source: Bacillus subtilis
• Cellular location: Cytoplasm: P17893
• Total number of polymer chains: 1
• Total formula weight: 7430.47

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.
A high-resolution structure of the DNA-binding domain of AhrC, the arginine repressor/activator protein from Bacillus subtilis.
Acta Crystallogr.,Sect.F, 63:914-917, 2007

PubMed Abstract: In Bacillus subtilis the concentration of L-arginine is controlled by the transcriptional regulator AhrC, which interacts with 18 bp DNA operator sites called ARG boxes in the promoters of arginine biosynthetic and catabolic operons. AhrC is a 100 kDa homohexamer, with each subunit having two domains. The C-terminal domains form the core, mediating intersubunit interactions and binding of the co-repressor L-arginine, whilst the N-terminal domains contain a winged helix-turn-helix DNA-binding motif and are arranged around the periphery. The N-terminal domain of AhrC has been expressed, purified and characterized and it has been shown that the fragment still binds DNA operators as a recombinant monomer. The DNA-binding domain has also been crystallized and the crystal structure refined to 1.0 A resolution is presented.

PubMed: 18007039
DOI: 10.1107/S1744309107048166

Experimental method

X-RAY DIFFRACTION (1 Å)