De novo structural modeling and computational sequence analysis of a bacteriocin protein isolated from Rhizobium leguminosarum bv. viciae strain LC-31

Abstract

Bacteriocins produced by different groups of bacteria are ribosomally synthesized peptides or proteins with antimicrobial and specific antagonistic bacterial interaction activity. Rhizobium leguminosarum is a Gram-negative soil bacterium which plays an important role in nitrogen fixation in leguminose plants. Bacteriocins produced by different strains of R. leguminosarum are known to impart antagonistic effects on other closely related strains. Recently, a bacteriocin gene was isolated from R. leguminosarum bv. viceae strain LC-31. Our study was aimed towards computational proteomic analysis and 3D structural modeling of this novel bacteriocin protein encoded by the earlier aforementioned gene. Different bioinformatics tools and machine learning techniques were used for protein structural classification. De novo protein modeling was performed by using I-TASSER server. The final model obtained was accessed by PROCHECK and DFIRE2, which confirmed that the final model is reliable. Until complete biochemical and structural data of bacteriocin protein produced by R. leguminosarum bv. viceae strain LC-31 are determined by experimental means, this model can serve as a valuable reference for characterizing this multifunctional protein.

Key words: Bacteriocin, rhizobium, protein modelling, nodulation, symbiosis, nitrogen fixation.