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

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.

Cite this paper

@article{Savitsky1998EvidenceFI, title={Evidence for indole-3-acetic acid binding site in plant peroxidases. Structural similarity between peroxidases and auxin-binding proteins.}, author={Pavel A. Savitsky and A. M. Rojkova and Vladimir I. Tishkov and Igor V Ouporov and Galina Nikolaevna Rudenskaya and Irina G. Gazaryan}, journal={Biochemistry. Biokhimii︠a︡}, year={1998}, volume={63 6}, pages={629-33} }