Mutation of a buried residue causes loss of activity but no conformational change in the heat-labile enterotoxin of Escherichia coli

Nat Struct Biol. 1995 Apr;2(4):269-72. doi: 10.1038/nsb0495-269.
No abstract available

Publication types

  • Comparative Study
  • Letter

MeSH terms

  • Amino Acid Sequence
  • Bacterial Toxins / chemistry*
  • Bacterial Toxins / toxicity*
  • Binding Sites
  • Crystallography, X-Ray
  • Enterotoxins / chemistry*
  • Enterotoxins / toxicity*
  • Escherichia coli
  • Escherichia coli Proteins*
  • Lysine
  • Macromolecular Substances
  • Models, Molecular
  • Mutagenesis, Site-Directed
  • Point Mutation
  • Protein Conformation*
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / toxicity
  • Valine

Substances

  • Bacterial Toxins
  • Enterotoxins
  • Escherichia coli Proteins
  • Macromolecular Substances
  • Recombinant Proteins
  • heat-labile enterotoxin, E coli
  • Valine
  • Lysine