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J Bacteriol. 1992 Oct;174(20):6707-10.

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

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  • 1Institut für Medizinische Mikrobiologie, Johannes-Gutenberg-Universität, Mainz, Federal Republic of Germany.

Abstract

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.

PMID:
1307487
[PubMed - indexed for MEDLINE]
PMCID:
PMC207659
Free PMC Article
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