PDBsum entry 1epw

Hydrolase

PDB id: 1epw

Contents

Protein chain

1287 a.a. *

Ligands

SO4

Metals

_ZN

Waters ×864

* Residue conservation analysis

PDB id:

1epw

Name:

Hydrolase

Title:

Crystal structure of clostridium neurotoxin type b

Structure:

Botulinum neurotoxin type b. Chain: a. Synonym: bontoxilysin b. Ec: 3.4.24.69

Source:

Clostridium botulinum. Organism_taxid: 1491

Resolution:

1.90Å R-factor: 0.202 R-free: 0.233

Authors:

S.Swaminathan,S.Eswaramoorthy

Key ref:

S.Swaminathan and S.Eswaramoorthy (2000). Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B. Nat Struct Biol, 7, 693-699. PubMed id: 10932256 DOI: 10.1038/78005

Date:

29-Mar-00 Release date: 01-Nov-00

Protein chain

P10844  (BXB_CLOBO) -  Botulinum neurotoxin type B from Clostridium botulinum

Seq: 1291 a.a.

Struc: 1287 a.a.

Enzyme reactions

• Enzyme class: E.C.3.4.24.69 - bontoxilysin.
• Reaction: Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No detected action on small molecule substrates.
• Cofactor: Zn(2+)

DOI no: 10.1038/78005

Nat Struct Biol 7:693-699 (2000)

PubMed id: 10932256

Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B.

S.Swaminathan, S.Eswaramoorthy.

ABSTRACT

Clostridium botulinum neurotoxins are among the most potent toxins to humans. The crystal structures of intact C. botulinum neurotoxin type B (BoNT/B) and its complex with sialyllactose, determined at 1. 8 and 2.6 A resolution, respectively, provide insight into its catalytic and binding sites. The position of the belt region in BoNT/B is different from that in BoNT/A; this observation presents interesting possibilities for designing specific inhibitors that could be used to block the activity of this neurotoxin. The structures of BoNT/B and its complex with sialyllactose provide a detailed description of the active site and a model for interactions between the toxin and its cell surface receptor. The latter may provide valuable information for recombinant vaccine development.

Selected figure(s)

Figure 3.
Figure 3. The active and binding sites of BoNT/B. a, Stereo view of the active site environment. Zinc and bonds to its coordinating residues are shown in orange. Residues in the first shell around the zinc (the immediate surroundings) are shown as ball and stick models, while residues in the second shell and water molecules are shown as ball and stick models with their van der Waals surfaces as dotted surfaces. Hydrogen bonds are shown as thin blue lines. b, Stereo view of sialyllactose and the residues interacting with it. Residues from a symmetry related molecule are shown in blue. Potential hydrogen bond contacts are shown as dashed lines.

Figure 6.
Figure 6. Sigma weighted 2F[o] - F[c] maps. a, A representative section of the 2F[o] - F[c] map of intact BoNT/B structure contoured at 1.2 . All reflections up to 1.8 Å resolution were included in the map calculations. b, 2F[o] - F[c] map showing density around sialyllactose contoured at 1.0 in the crystal structure of BoNT/B in complex with sialyllactose.

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (2000, 7, 693-699) copyright 2000.

Figures were selected by an automated process.