› 1x12

X-ray diffraction
2Å resolution

Structure of Mutant Pyrrolidone Carboxyl Peptidase (E192D) from a Hyperthermophile, Pyrococcus furiosus

Released:
DOI: 10.2210/pdb1x12/pdb
PDB entry 1x12 coloured by chain, front view.
PDB entry 1x12 coloured by chain, side view.
PDB entry 1x12 coloured by chain, top view.
Source organism: Pyrococcus furiosus
Primary publication:
Completely buried, non-ion-paired glutamic acid contributes favorably to the conformational stability of pyrrolidone carboxyl peptidases from hyperthermophiles.
Kaushik JK, Iimura S, Ogasahara K, Yamagata Y, Segawa S, Yutani K
Biochemistry 45 7100-12 (2006)
PMID: 16752900

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 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: 22.81 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: SPRING-8 BEAMLINE BL40B2
Spacegroup: P212121
Unit cell:
a: 47.451Å b: 103.845Å c: 187.056Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.214 0.239
Expression system: Escherichia coli

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Citations

3 review citations

The role of protonation states in ligand-receptor recognition and binding.
Petukh et al. (2013)
2 more