1f31

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Image:1f31.jpg

1f31, resolution 2.6Å

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CRYSTAL STRUCTURE OF CLOSTRIDIUM BOTULINUM NEUROTOXIN B COMPLEXED WITH A TRISACCHARIDE

Overview

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.

About this Structure

1F31 is a Single protein structure of sequence from Clostridium botulinum with and as ligands. Active as Bontoxilysin, with EC number 3.4.24.69 Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B., Swaminathan S, Eswaramoorthy S, Nat Struct Biol. 2000 Aug;7(8):693-9. PMID:10932256

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