STRUCTURAL DYNAMICS OF LACTOBACILLUS RHAMNOSUS PROTEINS UNDER COPPER SULPHATE AND ZINC CHLORIDE STRESS

Lactobacillus rhamnosus plays an important role as probiotic often associated with beneficial health effects. Although copper and zinc are trace metals, they are toxic at high concentrations. In this paper, bioinformatic tools and molecular modeling approach was adopted to explore the structure of L. rhamnosus under copper sulfate and zinc chloride stress. The differentially expressed proteins under stress were Aspartate kinase, Mannose-6-phosphate isomerase, Glutamate dehydrogenase, 30 S ribosomal subunit S19, 50 S ribosomal subunit L4, Pyruvate oxidase, Thymidylate synthase, and ATP dependent Clp protease ATP binding subunit ClpL. The homology models for these proteins were developed by using Modeller 9.5v. The models were validated by using protein structure checking tools PROCHECK. These structures will provide a good foundation for functional analysis of L. rhamnosus proteins against toxic metal pollutant. Another three differentially expressed proteins were also elevated namely Acetyltransferase, Alkaline shock protein, Cell division initiation protein Div IVA. But these protein structures were not predicted because Query coverage, identity, and E-values were not matched.