› 2zfz

X-ray diffraction
1.85Å resolution

Crystal structure of the C-terminal domain hexamer of ArgR from Mycobacterium tuberculosis in complex with arginine

Released:
DOI: 10.2210/pdb2zfz/pdb
PDB entry 2zfz coloured by chain, front view.
PDB entry 2zfz coloured by chain, side view.
PDB entry 2zfz coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
Structure of the C-terminal domain of the arginine repressor protein from Mycobacterium tuberculosis.
Cherney LT, Cherney MM, Garen CR, Lu GJ, James MN
Acta Crystallogr D Biol Crystallogr 64 950-6 (2008)
PMID: 18703843

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo hexamer
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162029 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arginine repressor Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 79 amino acids
Theoretical weight: 8.14 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WPY9 (Residues: 92-170; Coverage: 47%)
Gene names: MTCY06H11.22, Rv1657, ahrC, argR
Sequence domains: Arginine repressor, C-terminal domain
Structure domains: Gyrase A; domain 2

Ligands and Environments

2 bound ligands:
Ligand ARG 6 x ARG
Ligand GAI 2 x GAI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P212121
Unit cell:
a: 57.673Å b: 75.947Å c: 107.099Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.177 0.225
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

The structure of the arginine repressor from Mycobacterium tuberculosis bound with its DNA operator and Co-repressor, L-arginine.
Cherney et al. (2009)
3 more

2 mentions without citation

Symmetric allosteric mechanism of hexameric Escherichia coli arginine repressor exploits competition between L-arginine ligands and resident arginine residues.
Strawn et al. (2010)
1 more