› 1yvg

X-ray diffraction
2.6Å resolution

Structural analysis of the catalytic domain of tetanus neurotoxin

Released:
DOI: 10.2210/pdb1yvg/pdb
PDB entry 1yvg coloured by chain, front view.
PDB entry 1yvg coloured by chain, side view.
PDB entry 1yvg coloured by chain, top view.
Source organism: Clostridium tetani
Primary publication:
Structural analysis of the catalytic domain of tetanus neurotoxin.
Rao KN, Kumaran D, Binz T, Swaminathan S
Toxicon 45 929-39 (2005)
PMID: 15904688

Function and Biology Details

Reaction catalysed: 
Hydrolysis of -Gln(76)-|-Phe- bond in synaptobrevin (also known as neuronal vesicle-associated membrane protein, VAMP).
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138291 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tetanus toxin light chain Chain: A
Molecule details ›
Chain: A
Length: 468 amino acids
Theoretical weight: 53.7 KDa
Source organism: Clostridium tetani
Expression system: Escherichia coli
UniProt:
  • Canonical: P04958 (Residues: 2-458; Coverage: 35%)
Gene names: CTC_p60, tetX
Sequence domains: Clostridial neurotoxin zinc protease
Structure domains: Metalloproteases ("zincins"), catalytic domain like

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C, NSLS BEAMLINE X25
Spacegroup: C222
Unit cell:
a: 106.61Å b: 177.28Å c: 54.55Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.218 0.276
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Botulinum neurotoxin: a marvel of protein design.
Montal M. (2010)
6 more

5 mentions without citation

Bioinformatic discovery of a toxin family in Chryseobacterium piperi with sequence similarity to botulinum neurotoxins.
Mansfield et al. (2019)
4 more