› 5o3x

X-ray diffraction
2.55Å resolution

Structural characterization of the fast and promiscuous macrocyclase from plant - apo PCY1

Released:
DOI: 10.2210/pdb5o3x/pdb
PDB entry 5o3x coloured by chain, front view.
PDB entry 5o3x coloured by chain, side view.
PDB entry 5o3x coloured by chain, top view.
Source organism: Gypsophila vaccaria
Primary publication:
Characterization of the Fast and Promiscuous Macrocyclase from Plant PCY1 Enables the Use of Simple Substrates.
Ludewig H, Czekster CM, Oueis E, Munday ES, Arshad M, Synowsky SA, Bent AF, Naismith JH
OpenAccess logo ACS Chem Biol 13 801-811 (2018)
PMID: 29377663

Function and Biology Details

Reaction catalysed: 
Hydrolysis of --Pro-|- and to a lesser extent --Ala-|- in oligopeptides.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195780 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Prolyl endopeptidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 724 amino acids
Theoretical weight: 82.5 KDa
Source organism: Gypsophila vaccaria
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: R4P353 (Residues: 1-724; Coverage: 100%)
Gene name: Pcy1
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CAC 2 x CAC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: C2
Unit cell:
a: 275.58Å b: 60.85Å c: 88.04Å
α: 90° β: 92.65° γ: 90°
R-values:
R R work R free
0.219 0.216 0.263
Expression system: Escherichia coli BL21(DE3)

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Citations

5 review citations

New developments in RiPP discovery, enzymology and engineering.
Montalbán-López et al. (2021)
4 more

1 mention without citation

Characterization of the Fast and Promiscuous Macrocyclase from Plant PCY1 Enables the Use of Simple Substrates.
Ludewig et al. (2018)