Abstract
Lipoxygenase-1 (LOX-1) protein provides defense against pests and pathogens and its presence have been positively correlated with plant resistance against pathogens. Linoleate is a known substrate of lipoxygenase and it induces necrosis leading to the accumulation of isoflavonoid phytoalexins in plant leaves. Therefore, it is of interest to study the structural features of LOX-1 from Finger millet. However, the structure ofLOX-1 from Finger millet is not yet known. A homology model of LOX-1 from Finger millet is described. Domain architecture study suggested the presence of two domains namely PLAT (Phospho Lipid Acyl Transferase) and lipoxygenase. Molecular docking models of linoleate with lipoxygenase from finger millet, rice and sorghum are reported. The features of docked models showed that finger millet have higher pathogen resistance in comparison to other cereal crops. This data is useful for the molecular cloning of fulllength LOX-1 gene for validating its role in improving plant defense against pathogen infection and for various other biological processes.
Highlights
Lipoxygenases (Fatty-acid metabolism) are a class of ironcontaining and most widely studied enzymes that catalyze the hydroperoxidation of polyunsaturated fatty acids (PUFAs) in lipids containing a cis, cis-1, 4-pentadiene structure
Results & Discussion: In order to derive the 3D structure of lipoxygenase protein in finger millet, homology-modeling approach was used due to unavailability of experimental structure of this versatile protein
Phylogenetic analysis for template selection Lipoxygenase finger millet was taken as query sequence to perform local alignment search (Blastp) against protein data bank (PDB) for searching the homologous sequence and family belongingness
Summary
Lipoxygenases (Fatty-acid metabolism) are a class of ironcontaining and most widely studied enzymes that catalyze the hydroperoxidation of polyunsaturated fatty acids (PUFAs) in lipids containing a cis, cis-1, 4-pentadiene structure. LOX isoenzyme is almost uniformly present in the plant kingdom and it takes part in different physiological processes including flowering, seed germination, growth, development, pest resistance, and senescence or response to wound [2] These proteins perform their functions by protein-protein interaction and post translational modifications [8]. In silico analysis and homology modeling was used to characterize lipoxygenase protein in Finger millet. This method is much cost and time-effective compared to wet experimental techniques like X-ray crystallography and NMR. Functional characterization SMART database was used to identify the domain in lipoxygenase protein, which was used by CYS_REC program [28] to locate disulphide bridges “SS bond” between cysteine residues This tool provides the positions and total number of cysteine residues etc. This database provides a decisive evaluation of protein-protein interactions, including direct as well as indirect associations
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