PDBsum entry 2p5m

DNA binding protein

PDB id: 2p5m

Contents

Protein chains

82 a.a. *

Ligands

ARG ×5

Waters ×174

* Residue conservation analysis

PDB id:

2p5m

Name:

DNA binding protein

Title:

C-terminal domain hexamer of ahrc bound with l-arginine

Structure:

Arginine repressor. Chain: a, b, c. Fragment: c-terminal domain (residues 67-149). Synonym: arginine hydroxamate resistance protein. Engineered: yes. Mutation: yes

Source:

Bacillus subtilis. Organism_taxid: 1423. Gene: argr, ahrc. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

1.95Å R-factor: 0.187 R-free: 0.224

Authors:

J.A.Garnett,S.Baumberg,P.G.Stockley,S.E.V.Phillips

Key ref:

J.A.Garnett et al. (2007). Structure of the C-terminal effector-binding domain of AhrC bound to its corepressor L-arginine. Acta Crystallogr Sect F Struct Biol Cryst Commun, 63, 918-921. PubMed id: 18007040

Date:

15-Mar-07 Release date: 30-Oct-07

Protein chains

P17893  (ARGR_BACSU) -  Arginine repressor from Bacillus subtilis (strain 168)

Seq: 149 a.a.

Struc: 82 a.a.

Acta Crystallogr Sect F Struct Biol Cryst Commun 63:918-921 (2007)

PubMed id: 18007040

Structure of the C-terminal effector-binding domain of AhrC bound to its corepressor L-arginine.

J.A.Garnett, S.Baumberg, P.G.Stockley, S.E.Phillips.

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.