Evidence for indole-3-acetic acid binding site in plant peroxidases. Structural similarity between peroxidases and auxin-binding proteins.
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.
Department of Chemical Enzymology, School of Chemistry, Lomonosov Moscow State University, Moscow, 119899, Russia.
P A
PA
Savitsky
A M
AM
Rojkova
V I
VI
Tishkov
I V
IV
Ouporov
G N
GN
Rudenskaya
I G
IG
Gazaryan
D000595:Amino Acid Sequence; D007210:Indoleacetic Acids / Q000378:metabolism*; D008969:Molecular Sequence Data; D010544:Peroxidases / Q000737:chemistry / Q000378:metabolism*; D010937:Plant Growth Regulators; D010940:Plant Proteins; D010944:Plants / Q000201:enzymology*; D011487:Protein Conformation; D011956:Receptors, Cell Surface / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid
D007210:Indoleacetic Acids; D010937:Plant Growth Regulators; D010940:Plant Proteins; D011956:Receptors, Cell Surface; C046131:auxin receptor, plant; C030737:indoleacetic acid; D010544:Peroxidases