Evidence for a modular structure of the homologous repetitive C-terminal carbohydrate-binding sites of Clostridium difficile toxins and Streptococcus mutans glucosyltransferases.

AUTOR(ES)

von Eichel-Streiber, C

RESUMO

The homologous C-terminal repeats of Clostridium difficile toxins (ToxA and ToxB) and streptococcal glucosyltransferases appear to mediate protein-carbohydrate interactions at cellular binding sites with sugar moieties as substrates. A consensus sequence of 134 repeating units from gram-positive bacteria indicates that these repeats have a modular design with (i) a stretch of aromatic amino acids proposed to be involved in the primary carbohydrate-protein interaction, (ii) an amplification of this interaction by repetition of the respective sequences, and (iii) a second domain, not characterized, that is responsible for carbohydrate specificity.

Documentos Relacionados

• Role of C-terminal direct repeating units of the Streptococcus mutans glucosyltransferase-S in glucan binding.
• Carbohydrate-binding sites of the mannose-specific fimbrial lectins of enterobacteria.
• Identification of essential amino acids in the Streptococcus mutans glucosyltransferases.
• Screening for carbohydrate-binding proteins in extracts of Uruguayan plants
• Endogenous carbohydrate-binding proteins in Pneumocystis carinii.