› 4i9e

X-ray diffraction
2.4Å resolution

Crystal structure of Aspartyl phosphate phosphatase F from Bacillus subtilis

Released:
DOI: 10.2210/pdb4i9e/pdb
PDB entry 4i9e coloured by chain, front view.
PDB entry 4i9e coloured by chain, side view.
PDB entry 4i9e coloured by chain, top view.
Source organism: Bacillus subtilis subsp. subtilis str. 168
Primary publication:
Structural basis of Rap phosphatase inhibition by Phr peptides.
Gallego del Sol F, Marina A
PLoS Biol 11 e1001511 (2013)
PMID: 23526880

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159764 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Regulatory protein RapF Chains: A, B
Molecule details ›
Chains: A, B
Length: 383 amino acids
Theoretical weight: 45.79 KDa
Source organism: Bacillus subtilis subsp. subtilis str. 168
Expression system: Escherichia coli
UniProt:
  • Canonical: P71002 (Residues: 1-381; Coverage: 100%)
Gene names: BSU37460, rapF, ywhJ
Sequence domains:
Structure domains: Tetratricopeptide repeat domain

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC, FRU
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P3121
Unit cell:
a: 97.21Å b: 97.21Å c: 203.155Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.204 0.202 0.24
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Spore formation in Bacillus subtilis.
Tan et al. (2014)
7 more

5 mentions without citation

Structural Mechanisms of Peptide Recognition and Allosteric Modulation of Gene Regulation by the RRNPP Family of Quorum-Sensing Regulators.
Do et al. (2016)
4 more