4ux7

X-ray diffraction
2.55Å resolution

Structure of a Clostridium difficile sortase

Released:

Function and Biology Details

Reaction catalysed:
The enzyme catalyzes a cell wall sorting reaction in which a surface protein with a sorting signal containing a NPXTN motif is cleaved between the Thr and Asn residue. The resulting threonine carboxyl end of the protein is covalently attached to a pentaglycine cross-bridge of peptidoglycan.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-172673 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidase C60B, sortase B Chains: A, B
Molecule details ›
Chains: A, B
Length: 242 amino acids
Theoretical weight: 28.32 KDa
Source organism: Clostridioides difficile 630
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q183F3 (Residues: 33-225; Coverage: 86%)
Gene name: CD630_27180
Sequence domains: Sortase domain
Structure domains: Sortase

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P212121
Unit cell:
a: 38.247Å b: 90.273Å c: 134.738Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.196 0.262
Expression system: Escherichia coli BL21(DE3)