› 1skf

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE OF THE STREPTOMYCES K15 DD-TRANSPEPTIDASE

Released:
DOI: 10.2210/pdb1skf/pdb
PDB entry 1skf coloured by chain, front view.
PDB entry 1skf coloured by chain, side view.
PDB entry 1skf coloured by chain, top view.
Source organism: Streptomyces sp. K15
Primary publication:
The crystal structure of a penicilloyl-serine transferase of intermediate penicillin sensitivity. The DD-transpeptidase of streptomyces K15.
Fonzé E, Vermeire M, Nguyen-Distèche M, Brasseur R, Charlier P
J Biol Chem 274 21853-60 (1999)
PMID: 10419503

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153808 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
D-alanyl-D-alanine carboxypeptidase Chain: A
Molecule details ›
Chain: A
Length: 262 amino acids
Theoretical weight: 27.51 KDa
Source organism: Streptomyces sp. K15
UniProt:
  • Canonical: P39042 (Residues: 30-291; Coverage: 100%)
Sequence domains: D-alanyl-D-alanine carboxypeptidase
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 46.593Å b: 54.528Å c: 108.697Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.183 0.243

Quick links

Citations

5 review citations

The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis.
Sauvage et al. (2008)
4 more

6 mentions without citation

Cell Wall Hydrolases in Bacteria: Insight on the Diversity of Cell Wall Amidases, Glycosidases and Peptidases Toward Peptidoglycan.
Vermassen et al. (2019)
5 more