2P5M

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

2P5M の概要

• エントリーDOI: 10.2210/pdb2p5m/pdb
• 関連するPDBエントリー: 2P5K 2P5L
• 分子名称: Arginine repressor, ARGININE (3 entities in total)
• 機能のキーワード: alpha-beta, l-arginine binding domain, dna binding protein
• 由来する生物種: Bacillus subtilis
• 細胞内の位置: Cytoplasm: P17893
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 28745.84

構造登録者

Garnett, J.A.,Baumberg, S.,Stockley, P.G.,Phillips, S.E.V. (登録日: 2007-03-15, 公開日: 2007-10-30, 最終更新日: 2023-08-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.95 Å)