Affiliations: Department of Genetics, Osmania University, Hyderabad
– 500 007, India | Plant Molecular Biology Division, Institute of
Life-Sciences, Bhubaneswar – 751 023, India | Department of Botany, Utkal University, Vani Vihar,
Bhubaneswar – 751 004, India | Distributed Information Sub-Center, Institute of
Life-Sciences, Bhubaneswar-751 023, India
Note: [] Corresponding author: Institute of Life Sciences Nalco Square,
Chandrasekharpur, Bhubaneswar-751023, Orissa, India. E-mail: [email protected]
Abstract: Homology modeling of the catalase, CatC cloned and sequenced
from rice (Oryza sativa L., cv Ratna an Indica cultivar) has been
performed based on the crystal structure of the catalase CatF (PDB code
1m7s) by using the software MODELLER. With the aid of molecular mechanics and
molecular dynamics methods, the final model is obtained and is further assessed
by PROCHECK and VERIFY – 3D graph, which show that the final refined model is
reliable. With this model, a flexible docking study with the hydrogen peroxide,
the substrate for catalase, is performed and the results indicate that Arg310,
Asp343 and Arg346 in catalase are three important determinant residues in
binding as they have strong hydrogen bonding contacts with the substrate. These
hydrogen-bonding interactions play an important role for the stability of the
complex. Our results may be helpful for further experimental
investigations.
