1e1h
From Proteopedia
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CRYSTAL STRUCTURE OF RECOMBINANT BOTULINUM NEUROTOXIN TYPE A LIGHT CHAIN, SELF-INHIBITING ZN ENDOPEPTIDASE.
Overview
Clostridium botulinum neurotoxins (BoNTs), the most potent toxins known, disrupt neurotransmission through proteolysis of proteins involved in, neuroexocytosis. The light chains of BoNTs are unique zinc proteases that, have stringent substrate specificity and require exceptionally long, substrates. We have determined the crystal structure of the protease, domain from BoNT serotype A (BoNT/A). The structure reveals a homodimer in, a product-bound state, with loop F242-V257 from each monomer deeply buried, in its partner's catalytic site. The loop, which acts as a substrate, is, oriented in reverse of the canonical direction for other zinc proteases., The Y249-Y250 peptide bond of the substrate loop is hydrolyzed, leaving, the Y249 product carboxylate coordinated to the catalytic zinc. From ... [(full description)]
About this Structure
1E1H is a [Protein complex] structure of sequences from [Clostridium botulinum] with ZN as [ligand]. Active as [Bontoxilysin], with EC number [3.4.24.69]. Structure known Active Site: 1. Full crystallographic information is available from [OCA].
Reference
Crystal structure of Clostridium botulinum neurotoxin protease in a product-bound state: Evidence for noncanonical zinc protease activity., Segelke B, Knapp M, Kadkhodayan S, Balhorn R, Rupp B, Proc Natl Acad Sci U S A. 2004 May 4;101(18):6888-93. Epub 2004 Apr 23. PMID:15107500
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