› 4a5n

X-ray diffraction
1.81Å resolution

Redoxregulator HypR in its reduced form

Released:
DOI: 10.2210/pdb4a5n/pdb
PDB entry 4a5n coloured by chain, front view.
PDB entry 4a5n coloured by chain, side view.
PDB entry 4a5n coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Structural insights into the redox-switch mechanism of the MarR/DUF24-type regulator HypR.
Palm GJ, Khanh Chi B, Waack P, Gronau K, Becher D, Albrecht D, Hinrichs W, Read RJ, Antelmann H
Nucleic Acids Res 40 4178-92 (2012)
PMID: 22238377

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153416 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Uncharacterized HTH-type transcriptional regulator YybR Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 131 amino acids
Theoretical weight: 15.57 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P37486 (Residues: 1-125; Coverage: 100%)
Gene names: BSU40540, yybR
Sequence domains: HxlR-like helix-turn-helix
Structure domains: Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain

Ligands and Environments

2 bound ligands:
Ligand BME 4 x BME
Ligand EDO 1 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: P21
Unit cell:
a: 54.93Å b: 68.03Å c: 60.42Å
α: 90° β: 97.45° γ: 90°
R-values:
R R work R free
0.185 0.183 0.223
Expression system: Escherichia coli BL21

Quick links

Citations

6 review citations

Thiol-based redox switches in prokaryotes.
Hillion et al. (2015)
5 more

4 mentions without citation

Entropy redistribution controls allostery in a metalloregulatory protein.
Capdevila et al. (2017)
3 more