1yvg
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(New page: 200px<br /><applet load="1yvg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yvg, resolution 2.6Å" /> '''Structural analysis o...)
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Revision as of 04:57, 21 November 2007
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Structural analysis of the catalytic domain of tetanus neurotoxin
Overview
Clostridium neurotoxins, comprising the tetanus neurotoxin and the seven, antigenically distinct botulinum neurotoxins (BoNT/A-G), are among the, known most potent bacterial protein toxins to humans. Although they have, similar function, sequences and three-dimensional structures, the, substrate specificity and the selectivity of peptide bond cleavage are, different and unique. Tetanus and botulinum type B neurotoxins, enzymatically cleave the same substrate, vesicle-associated membrane, protein, at the same peptide bond though the optimum length of substrate, peptide required for cleavage by them is different. Here, we present the, first experimentally determined three-dimensional structure of the, catalytic domain of tetanus neurotoxin and analyze its active site. The, structure provides insight into the active site of tetanus toxin's, proteolytic activity and the importance of the nucleophilic water and the, role of the zinc ion. The probable reason for different modes of binding, of vesicle-associated membrane protein to botulinum neurotoxin type B and, the tetanus toxin is discussed. The structure provides a basis for, designing a novel recombinant vaccine or structure-based drugs for, tetanus.
About this Structure
1YVG is a Single protein structure of sequence from Clostridium tetani with ZN as ligand. Active as Tentoxilysin, with EC number 3.4.24.68 Full crystallographic information is available from OCA.
Reference
Structural analysis of the catalytic domain of tetanus neurotoxin., Rao KN, Kumaran D, Binz T, Swaminathan S, Toxicon. 2005 Jun 1;45(7):929-39. Epub 2005 Apr 13. PMID:15904688
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