Evidence for indole-3-acetic acid binding site in plant peroxidases. Structural similarity between peroxidases and auxin-binding proteins

Biochemistry (Mosc). 1998 Jun;63(6):629-33.

Abstract

Application of computer methods allowed us to demonstrate that plant peroxidases and auxin-binding proteins contain structurally similar fragments. The mapping of the fragments was done using a model structure of horseradish peroxidase. Five of six structurally similar fragments belong to the distal domain and form a subdomain in plant peroxidases that includes the distal heme-coordinating sequence, LHFHDC (amino acid residues 39-44 in horseradish peroxidase). The existence of a substrate-binding site for indole-3-acetic acid in the distal subdomain comprising helices A (whole), B (middle), C (beginning), and D (whole) and the loop between helices D and D' is discussed.

MeSH terms

  • Amino Acid Sequence
  • Indoleacetic Acids / metabolism*
  • Molecular Sequence Data
  • Peroxidases / chemistry
  • Peroxidases / metabolism*
  • Plant Growth Regulators*
  • Plant Proteins*
  • Plants / enzymology*
  • Protein Conformation
  • Receptors, Cell Surface / chemistry*
  • Sequence Homology, Amino Acid

Substances

  • Indoleacetic Acids
  • Plant Growth Regulators
  • Plant Proteins
  • Receptors, Cell Surface
  • auxin receptor, plant
  • indoleacetic acid
  • Peroxidases