› 1mvo

X-ray diffraction
1.6Å resolution

Crystal structure of the PhoP receiver domain from Bacillus subtilis

Released:
DOI: 10.2210/pdb1mvo/pdb
PDB entry 1mvo coloured by chain, front view.
PDB entry 1mvo coloured by chain, side view.
PDB entry 1mvo coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
The crystal structure of the phosphorylation domain in PhoP reveals a functional tandem association mediated by an asymmetric interface.
Birck C, Chen Y, Hulett FM, Samama JP
J Bacteriol 185 254-61 (2003)
PMID: 12486062

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146761 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alkaline phosphatase synthesis transcriptional regulatory protein PhoP Chain: A
Molecule details ›
Chain: A
Length: 136 amino acids
Theoretical weight: 15.55 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P13792 (Residues: 1-135; Coverage: 56%)
Gene names: BSU29110, phoP
Sequence domains: Response regulator receiver domain
Structure domains: Rossmann fold

Ligands and Environments

2 bound ligands:
Ligand MN 1 x MN
Ligand NA 2 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P41212
Unit cell:
a: 45.704Å b: 45.704Å c: 134.811Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.186 0.232
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Transcriptomic studies of phosphate control of primary and secondary metabolism in Streptomyces coelicolor.
Martín et al. (2012)
26 other articles

11 mentions without citation

Emerging Pharmacotherapeutic Strategies to Overcome Undruggable Proteins in Cancer.
Lu et al. (2023)
10 more