Modeling of PrnD protein from Pseudomonas fluorescens RajNB11 and its comparative structural analysis with PrnD proteins expressed in Burkholderia and Serratia

Pyrrolnitrin is produced by Pseudomonas fluorescens and plays an important role in control of pathogenic fungi. The prnABCD gene cluster codes for enzymes involved in biosynthesis of pyrrolnitrin. | Turkish Journal of Biology Turk J Biol (2016) 40: 623-633 © TÜBİTAK doi: Research Article Modeling of PrnD protein from Pseudomonas fluorescens RajNB11 and its comparative structural analysis with PrnD proteins expressed in Burkholderia and Serratia 1 2 3 1, Ram Nageena SINGH , Raghvendra Pratap SINGH , Anjana SHARMA , Anil Kumar SAXENA * 1 Division of Microbiology, Indian Agricultural Research Institute, Pusa, New Delhi, India 2 Microbial Genomics Resource Repository, National Bureau of Agriculturally Important Microorganisms, Kushmaur, Maunath Bhanjan, India 3 Department of Post Graduate Studies and Research in Biological Science, Rani Durgavati Vishwavidyalaya, Saraswati Vihar, Pachpedi, Jabalpur, India Received: Accepted/Published Online: Final Version: Abstract: Pyrrolnitrin is produced by Pseudomonas fluorescens and plays an important role in control of pathogenic fungi. The prnABCD gene cluster codes for enzymes involved in biosynthesis of pyrrolnitrin. Among the four genes, prnD is very important as it codes for arylamine N-oxygenase, the only biochemically characterized oxygenase involved in oxidation of the amino group of aminopyrrolnitrin to a nitro group to form pyrrolnitrin. A strain of Pseudomonas fluorescens RajNB11 efficient for antifungal activity was found to produce pyrrolnitrin. The prnD gene product of P. fluorescens RajNB11 that catalyzes the final step of production of pyrrolnitrin was characterized in the present study with regards to its stability and catalytic activity. The prnD gene was amplified from RajNB11, sequenced, translated, and 3-D modeled to its protein structure. The modeled protein of the test organism was compared to PrnD proteins of Burkholderia sp. and Serratia sp. The protein from P. fluorescens was found to be basic, hydrophilic with higher thermal stability, and easily separated after expression and purification. The .

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