› 5l8s

X-ray diffraction
2.5Å resolution

The crystal structure of a cold-adapted acylaminoacyl peptidase reveals a novel quaternary architecture based on the arm-exchange mechanism

Released:
DOI: 10.2210/pdb5l8s/pdb
PDB entry 5l8s coloured by chain, front view.
PDB entry 5l8s coloured by chain, side view.
PDB entry 5l8s coloured by chain, top view.
Source organism: Sporosarcina psychrophila
Primary publication:
A bacterial acyl aminoacyl peptidase couples flexibility and stability as a result of cold adaptation.
Brocca S, Ferrari C, Barbiroli A, Pesce A, Lotti M, Nardini M
FEBS J 283 4310-4324 (2016)
PMID: 27739253

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-122803 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amino acyl peptidase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 604 amino acids
Theoretical weight: 69.19 KDa
Source organism: Sporosarcina psychrophila
Expression system: Escherichia coli
UniProt:
  • Canonical: E1VFE0 (Residues: 1-596; Coverage: 100%)
Gene name: aph
Sequence domains: Prolyl oligopeptidase family

Ligands and Environments

1 bound ligand:
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 148.08Å b: 151.1Å c: 191.23Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.212 0.248
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Cold-Active β-Galactosidases: Insight into Cold Adaption Mechanisms and Biotechnological Exploitation.
Mangiagalli et al. (2021)
1 more

1 mention without citation

A bacterial acyl aminoacyl peptidase couples flexibility and stability as a result of cold adaptation.
Brocca et al. (2016)