› 2n6j

Solution NMR

Solution structure of Zmp1, a zinc-dependent metalloprotease secreted by Clostridium difficile

Released:
DOI: 10.2210/pdb2n6j/pdb
PDB entry 2n6j coloured by chain, ensemble of 20 models, front view.
PDB entry 2n6j coloured by chain, ensemble of 20 models, side view.
PDB entry 2n6j coloured by chain, ensemble of 20 models, top view.
Source organism: Clostridioides difficile 630
Primary publication:
Structural characterization of zinc-bound Zmp1, a zinc-dependent metalloprotease secreted by Clostridium difficile.
Rubino JT, Martinelli M, Cantini F, Castagnetti A, Leuzzi R, Banci L, Scarselli M
J Biol Inorg Chem 21 185-96 (2016)
PMID: 26711661

Function and Biology Details

Reaction catalysed: 
The enzyme catalyzes the hydrolytic cleavage of peptide bonds between two proline residues
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172683 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pro-Pro endopeptidase Chain: A
Molecule details ›
Chain: A
Length: 195 amino acids
Theoretical weight: 21.63 KDa
Source organism: Clostridioides difficile 630
Expression system: Escherichia coli
UniProt:
  • Canonical: Q183R7 (Residues: 27-220; Coverage: 100%)
Gene names: CD630_28300, ppep-1, zmp1
Sequence domains: Anthrax toxin lethal factor, N- and C-terminal domain

Ligands and Environments

1 bound ligand:
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 91%
Refinement method: torsion angle dynamics, molecular dynamics
Expression system: Escherichia coli

Quick links

Citations

2 review citations

The fed-batch principle for the molecular biology lab: controlled nutrient diets in ready-made media improve production of recombinant proteins in Escherichia coli.
Krause et al. (2016)
1 more

1 mention without citation

Discovery of a new Pro-Pro endopeptidase, PPEP-2, provides mechanistic insights into the differences in substrate specificity within the PPEP family.
Klychnikov et al. (2018)