Specific binding of nucleotides and NAD+ to Clostridium difficile toxin A

FEBS Lett. 1992 Feb 24;298(2-3):185-7. doi: 10.1016/0014-5793(92)80052-i.

Abstract

Binding of nucleotides, a tetrapolyphosphate, and NAD+ to purified toxin A of Clostridium difficile was determined by monitoring changes in intrinsic fluorescence following excitation at 280 nm, and recording emissions at 340 nm. Binding was specific for concentrations over the range 5 to 100 microM for ATP, GTP, and their respective non-hydrolysable analogues AMP-PNP and Gpp(NH)p, tetrapolyphosphate and NAD+.

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Amino Acid Sequence
  • Bacterial Toxins / metabolism*
  • Binding Sites
  • Clostridioides difficile / metabolism*
  • Enterotoxins / chemistry
  • Enterotoxins / metabolism*
  • Guanosine Triphosphate / metabolism
  • Molecular Sequence Data
  • NAD / metabolism*
  • Nucleotides / metabolism*
  • Protein Conformation
  • Spectrometry, Fluorescence
  • Tryptophan / chemistry

Substances

  • Bacterial Toxins
  • Enterotoxins
  • Nucleotides
  • tcdA protein, Clostridium difficile
  • NAD
  • Guanosine Triphosphate
  • Tryptophan
  • Adenosine Triphosphate