Structural characterization of a novel luciferase-like-monooxygenase from Pseudomonas meliae an in silico approach

Abstract

BackgroundLuciferase is a well-known oxidative enzyme that produces bioluminescence. The Pseudomonas meliae is a plant pathogen that causes wood rot on nectarine and peach and possesses a luciferase-like monooxygenase. After activation, it produces bioluminescence, and the pathogens bioluminescence is a visual indicator of diseased plants. MethodsThe present study aims to model and characterize the luciferase-like monooxygenase protein in P. meliae for its similarity to well-established luciferase. In this study, the luciferase-like monooxygenase from P. meliae infects chinaberry plants has been modeled first and then studied by comparing it with existing known luciferase. Also, the similarities between uncharacterized luciferase from P. meliae and template from Geobacillus thermodenitrificans were analyzed to find the novelty of P. meliae. ResultsThe results suggest that the absence of bioluminescence in P. meliae could be due to the evolutionary mutation in positions 138 and 311. The active site remains identical except for two amino acids; P. meliae Tyr138 instead of His138 and Leu311 instead of His311. Therefore, the P. meliae will have a potential future application, and mutation of the residues 138 and 311 can be restored luciferase light-emitting ability. ConclusionsThis study will help further improve, activate, and repurpose the luciferase from P. meliae as a reporter for gene expression.