6yj2

X-ray diffraction
2Å resolution

Structural and DNA binding studies of the transcriptional repressor Rv2506 (BkaR) from Mycobacterium tuberculosis supports a role in L-Leucine catabolism

Released:
Entry authors: Keep NH, Pritchard JE, Sula A, Cole AR, Kendall SL

Function and Biology Details

Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
HTH tetR-type domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 215 amino acids
Theoretical weight: 23.25 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O06169 (Residues: 1-215; Coverage: 100%)
Gene name: Rv2506
Sequence domains: Tetracyclin repressor-like, C-terminal domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: C2
Unit cell:
a: 181.764Å b: 52.874Å c: 91.919Å
α: 90° β: 90.1° γ: 90°
R-values:
R R work R free
0.194 0.192 0.224
Expression system: Escherichia coli BL21(DE3)