4ks6

X-ray diffraction
1.93Å resolution

Crystal structure of the catalytic domain of botulinum neurotoxin BoNT/A C134S mutant with covalent inhibitor that modifies Cys-165 causing disorder in 166-174 stretch

Released:
Entry authors: Stura EA, Vera L, Guitot K, Dive V

Function and Biology Details

Reaction catalysed:
Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevin (also known as neuronal vesicle-associated membrane protein, VAMP), synaptosome-associated protein of 25 kDa (SNAP25) or syntaxin. No detected action on small molecule substrates.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-144084 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Botulinum neurotoxin A light chain Chain: A
Molecule details ›
Chain: A
Length: 445 amino acids
Theoretical weight: 50.89 KDa
Source organism: Clostridium botulinum A str. Hall
Expression system: Escherichia coli
UniProt:
  • Canonical: P0DPI1 (Residues: 1-425; Coverage: 33%)
Gene names: CBO0806, CLC_0862, bna, botA
Sequence domains: Clostridial neurotoxin zinc protease
Structure domains: Metalloproteases ("zincins"), catalytic domain like
Peptide inhibitor MPT-DPP-DAR-G-DPN-NH2 Chain: B
Molecule details ›
Chain: B
Length: 6 amino acids
Theoretical weight: 552 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P43212
Unit cell:
a: 65.634Å b: 65.634Å c: 201.725Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.193 0.252
Expression systems:
  • Escherichia coli
  • Not provided