Structural analysis of the catalytic domain of tetanus neurotoxin

摘要: Clostridium neurotoxins, comprising the tetanus neurotoxin and seven antigenically distinct botulinum neurotoxins (BoNT/A-G), are among known most potent bacterial protein toxins to humans. Although they have similar function, sequences three-dimensional structures, substrate specificity selectivity of peptide bond cleavage different unique. Tetanus type B enzymatically cleave same substrate, vesicle-associated membrane protein, at though optimum length required for by them is different. Here, we present first experimentally determined structure catalytic domain analyze its active site. The provides insight into site toxin's proteolytic activity importance nucleophilic water role zinc ion. probable reason modes binding toxin discussed. a basis designing novel recombinant vaccine or structure-based drugs tetanus.