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Modelling of PrnD protein from Pseudomonas fluorescens rajNB11 and its comparative structural analysis with prnD proteins expressed in Burkholderia and Serratia

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Title Modelling of PrnD protein from Pseudomonas fluorescens rajNB11 and its comparative structural analysis with prnD proteins expressed in Burkholderia and Serratia
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Creator Singh RN, Singh RP, Sharma A and Saxena AK
 
Subject Pseudomonas fluorescens, pyrrolnitrin, cloning, protein modeling
 
Description Not Available
yrrolnitrin 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 pyrrolnitin. The prnD gene product of P. fluorescens RajNB11, that catalyses 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 protein structure. The modeled protein of 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 protein of P. fluorescens was found to have better folded structure, more serine residues in the active site, better active site properties and iso-electric point value in comparison to PrnD proteins of Burkholderia and Serratia.
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Date 2021-09-22T09:27:41Z
2021-09-22T09:27:41Z
2016-01-01
 
Type Research Paper
 
Identifier Not Available
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http://krishi.icar.gov.in/jspui/handle/123456789/64581
 
Language English
 
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Publisher Not Available