Computational studies on photolyase (Phr) proteins of cyanobacteria

Abstract

Photolyases (Phrs) are enzymes that utilize blue/ultraviolet (UV-A) region of light for repairing UV-induced cyclopyramidine dimer. We have studied Phr groups by bioinformatic analyses as well as active-site and structural modeling. The analysis of 238 amino acid sequences from 85 completely sequenced cyanobacterial genomes revealed five classes of Phrs, i.e., CPD Gr I, 6-4 Phrs/cryptochrome, Cry-DASH, Fe-S bacteria Phrs, and a group having fewer number of amino acids (276-385) in length. Distribution of Phr groups in cyanobacteria belonging to the order Synechococcales was found to be influenced by the habitats of the organisms. Class V Phrs were exclusively present in cyanobacteria. Unique motif and binding sites were reported in Group II and III. Fe-S protein binding site was only present in Group V. Active site residues and putative CPD/6-4pp binding residues are charged amino acids which were present on the surface of the proteins. Majority of hydrophilic amino acid residues were present on surface of Phrs. Sequence analysis confirmed the diverse nature of Phrs, though, sequence diversity does not affect their overall 3D structure. Protein-ligand interaction analysis identified novel CPD/6-4PP binding sites on Phrs. This structural information of Phrs can be used for the preparation of efficient Phr based formulations.