Computational protein structure modeling and analysis of UV-B stress protein in Synechocystis PCC 6803

This study focuses on Ultra Violet stress (UVS) gene product which is a UV stress induced protein from cyanobacteria,Synechocystis PCC 6803. Three dimensional structural modeling of target UVS protein was carried out by homology modelingmethod. 3F2I pdb from Nostoc sp. PCC 7120 was selected as a suitable template protein structure. Ultimately, the detection of activebinding regions was carried out for characterization of functional sites in modeled UV-B stress protein. The top five probableligand binding sites were predicted and the common binding residues between target and template protein was analyzed. It hasbeen validated for the first time that modeled UVS protein structure from Synechocystis PCC 6803 was structurally and functionallysimilar to well characterized UVS protein of another cyanobacterial species, Nostoc sp PCC 7120 because of having same structuralmotif and fold with similar protein topology and function. Investigations revealed that UVS protein from Synechocystis sp. mightplay significant role during ultraviolet resistance. Thus, it could be a potential biological source for remediation for UV inducedstress.