› 3ogg

X-ray diffraction
1.65Å resolution

Crystal structure of the receptor binding domain of botulinum neurotoxin D

Released:
DOI: 10.2210/pdb3ogg/pdb
PDB entry 3ogg coloured by chain, front view.
PDB entry 3ogg coloured by chain, side view.
PDB entry 3ogg coloured by chain, top view.
Source organism: Clostridium botulinum
Primary publication:
Structural analysis of the receptor binding domain of botulinum neurotoxin serotype D.
Zhang Y, Buchko GW, Qin L, Robinson H, Varnum SM
Biochem Biophys Res Commun 401 498-503 (2010)
PMID: 20858456

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148553 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Botulinum neurotoxin D heavy chain Chain: A
Molecule details ›
Chain: A
Length: 414 amino acids
Theoretical weight: 48.12 KDa
Source organism: Clostridium botulinum
Expression system: Escherichia coli
UniProt:
  • Canonical: P19321 (Residues: 863-1276; Coverage: 32%)
Gene name: botD
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P212121
Unit cell:
a: 60.782Å b: 89.68Å c: 93.929Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.173 0.172 0.192
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Botulinum neurotoxins: mechanism of action.
Tighe et al. (2013)
2 more

3 mentions without citation

Crystal structure of the receptor binding domain of the botulinum C-D mosaic neurotoxin reveals potential roles of lysines 1118 and 1136 in membrane interactions.
Zhang et al. (2011)
2 more