› 3cag

X-ray diffraction
1.9Å resolution

Crystal structure of the oligomerization domain hexamer of the arginine repressor protein from Mycobacterium tuberculosis in complex with 9 arginines.

Released:
DOI: 10.2210/pdb3cag/pdb
PDB entry 3cag coloured by chain, front view.
PDB entry 3cag coloured by chain, side view.
PDB entry 3cag 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

1 bound ligand:
Ligand ARG 9 x ARG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P212121
Unit cell:
a: 57.745Å b: 75.648Å c: 108.022Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.168 0.224
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

Biophysical characterization of the signature domains of thrombospondin-4 and thrombospondin-2.
Misenheimer et al. (2005)
1 more