Objective: To carry out in-silico sequence and structural analysis of flavin mononucleotide binding domain (FMN) of Pseudomonas aeruginosa nitroreductase enzyme which is of biotechnological significance and Comparison with its structural analogues
Methods: The FMN domain from Pseudomonas aeruginosa nitro reductase gene was cloned and sequenced. The sequence was subjected to multiple alignment, homology modeling and Ramchandran analysis with close structural homologues of nitro reductase as well as with that of phylogenetically related species.
Results: FMN binding site in case of Pseudomonas aeruginosa nitro reductase is more like the structural analogues B. subtilis, T. thermophilus and S. pneumoniae nitro reductases; conservation scores are mostly>6. However, the dimer interface sites are observed to be variable in nature. The phylogenetically related and diverse FMN domains were also analyzed with respect to conservation and variation of sequence
Conclusions: The conservation or variations of amino acids at the dimer interface would have implications in varied conformations of FMN binding domain inferring difference in function and kinetics of catalysis.
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