› 4wo7

X-ray diffraction
2.63Å resolution

Crystal Structure of PrsA from Bacillus subtilis

Released:
DOI: 10.2210/pdb4wo7/pdb
PDB entry 4wo7 coloured by chain, front view.
PDB entry 4wo7 coloured by chain, side view.
PDB entry 4wo7 coloured by chain, top view.
Source organism: Bacillus subtilis subsp. subtilis str. 168
Primary publication:
Dimeric Structure of the Bacterial Extracellular Foldase PrsA.
Jakob RP, Koch JR, Burmann BM, Schmidpeter PA, Hunkeler M, Hiller S, Schmid FX, Maier T
J Biol Chem 290 3278-92 (2015)
PMID: 25525259

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150211 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Foldase protein PrsA Chains: A, B
Molecule details ›
Chains: A, B
Length: 263 amino acids
Theoretical weight: 29.98 KDa
Source organism: Bacillus subtilis subsp. subtilis str. 168
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P24327 (Residues: 21-280; Coverage: 95%)
Gene names: BSU09950, prsA
Sequence domains: PPIC-type PPIASE domain

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 10 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: C2221
Unit cell:
a: 69.29Å b: 87.68Å c: 234.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.228 0.226 0.251
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Prolyl isomerization and its catalysis in protein folding and protein function.
Schmidpeter et al. (2015)
3 more

7 mentions without citation

The Blueprint of a Minimal Cell: MiniBacillus.
Reuß et al. (2016)
6 more