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PMID: 1307487 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

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

Journal of bacteriology ·Vol. 174 ·No. 20 ·1992-10-00 ·Pages 6707-10

von Eichel-Streiber C, Sauerborn M, Kuramitsu HK

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.

MeSH Terms
Amino Acid Sequence Bacterial Proteins/chemistry,metabolism Bacterial Toxins/chemistry,metabolism Binding Sites Carbohydrate Metabolism Clostridioides difficile/chemistry Consensus Sequence Cytotoxins/chemistry Enterotoxins/chemistry,metabolism Glucosyltransferases/chemistry,metabolism Molecular Sequence Data Sequence Homology, Amino Acid Streptococcus mutans/enzymology
Chemicals
Bacterial Proteins Bacterial Toxins Cytotoxins Enterotoxins tcdA protein, Clostridium difficile toxB protein, Clostridium difficile Glucosyltransferases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
von Eichel-Streiber C
Institut für Medizinische Mikrobiologie, Johannes-Gutenberg-Universität, Mainz, Federal Republic of Germany.
Sauerborn M
Kuramitsu H K
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/jb.174.20.6707-6710.1992
Published
1992-10-00
Pages
6707-10
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC207659
Subset
IM
Grants
NIDCR NIH HHS · DE03258 · United States
External Links
PubMed source DOI: 10.1128/jb.174.20.6707-6710.1992 PMC Full Text View journal details
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