Cross-Species Insights into PR Proteins: A Comprehensive Study of , , and .

UNLABELLED

This study provides a comprehensive analysis of pathogenesis-related (PR) proteins, focusing on PR1, PR5, and PR10, in three plant species: (At), (Sl), and (St). We investigated various physico-chemical properties, including protein length, molecular weight, isoelectric point (pI), hydrophobicity, and structural characteristics, such as RMSD, using state-of-the-art tools like AlphaFold and PyMOL. Our analysis found that the SlPR10-StPR10 protein pair had the highest sequence identity (80.00%), lowest RMSD value (0.307 Å), and a high number of overlapping residues (160) among all other protein pairs, indicating their remarkable similarity. Additionally, we used bioinformatics tools such as Cello, Euk-mPLoc 2.0, and Wolfpsort to predict subcellular localization, with AtPR1, AtPR5, and SlPR5 proteins predicted to be located in the extracellular space in both and , while AtPR10 was predicted to be located in the cytoplasm. This comprehensive analysis, including the use of cutting-edge structural prediction and subcellular localization tools, enhances our understanding of the structural, functional, and localization aspects of PR proteins, shedding light on their roles in plant defense mechanisms across different plant species.

SUPPLEMENTARY INFORMATION

The online version contains supplementary material available at 10.1007/s12088-024-01343-1.