› 1iof

X-ray diffraction
2.2Å resolution

X-RAY CRYSTALLINE STRUCTURES OF PYRROLIDONE CARBOXYL PEPTIDASE FROM A HYPERTHERMOPHILE, PYROCOCCUS FURIOSUS, AND ITS CYS-FREE MUTANT

Released:
DOI: 10.2210/pdb1iof/pdb
PDB entry 1iof coloured by chain, front view.
PDB entry 1iof coloured by chain, side view.
PDB entry 1iof coloured by chain, top view.
Source organism: Pyrococcus furiosus
Primary publication:
X-ray crystalline structures of pyrrolidone carboxyl peptidase from a hyperthermophile, Pyrococcus furiosus, and its cys-free mutant.
Tanaka H, Chinami M, Mizushima T, Ogasahara K, Ota M, Tsukihara T, Yutani K
J Biochem 130 107-18 (2001)
PMID: 11432786

Function and Biology Details

Reaction catalysed: 
Release of an N-terminal pyroglutamyl group from a polypeptide, the second amino acid generally not being Pro.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130730 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyrrolidone-carboxylate peptidase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 208 amino acids
Theoretical weight: 22.85 KDa
Source organism: Pyrococcus furiosus
Expression system: Escherichia coli
UniProt:
  • Canonical: O73944 (Residues: 1-208; Coverage: 100%)
Gene names: PF1299, pcp
Sequence domains: Pyroglutamyl peptidase
Structure domains: Peptidase C15, pyroglutamyl peptidase I-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 57.9Å b: 105Å c: 78.5Å
α: 90° β: 90.7° γ: 90°
R-values:
R R work R free
0.195 0.195 0.232
Expression system: Escherichia coli

Quick links

Citations

14 citation in other articles

Recent progress towards the application of hyperthermophiles and their enzymes.
Atomi H. (2005)
13 more

2 mentions without citation

"Hot cores" in proteins: comparative analysis of the apolar contact area in structures from hyper/thermophilic and mesophilic organisms.
Paiardini et al. (2008)
1 more