› 1dfq

X-ray diffraction
2.6Å resolution

THE HC FRAGMENT OF TETANUS TOXIN COMPLEXED WITH SIALIC ACID

Released:
DOI: 10.2210/pdb1dfq/pdb
PDB entry 1dfq coloured by chain, front view.
PDB entry 1dfq coloured by chain, side view.
PDB entry 1dfq coloured by chain, top view.
Source organism: Clostridium tetani
Primary publication:
The structures of the H(C) fragment of tetanus toxin with carbohydrate subunit complexes provide insight into ganglioside binding.
Emsley P, Fotinou C, Black I, Fairweather NF, Charles IG, Watts C, Hewitt E, Isaacs NW
J Biol Chem 275 8889-94 (2000)
PMID: 10722735

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138291 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tetanus toxin heavy chain Chain: A
Molecule details ›
Chain: A
Length: 444 amino acids
Theoretical weight: 50.84 KDa
Source organism: Clostridium tetani
Expression system: Escherichia coli
UniProt:
  • Canonical: P04958 (Residues: 872-1315; Coverage: 34%)
Gene names: CTC_p60, tetX
Sequence domains:
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: P212121
Unit cell:
a: 66.86Å b: 70.24Å c: 122.52Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.2 0.313
Expression system: Escherichia coli

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Citations

17 review citations

Botulinum and tetanus neurotoxins: structure, function and therapeutic utility.
Turton et al. (2002)
16 more

3 mentions without citation

Tetanus Toxin Fragment C: Structure, Drug Discovery Research and Production.
Bayart et al. (2022)
2 more