One of the common studies on industrial proteins is to study the RNA Folding and stability, protein stability, physicochemical properties and conformational structure. In our previous proteomics study, Metallopeptidase (MP) was isolated from Lactobacillus casei, which in this study, it was evaluated with RNA fold, Protparam, I-TASSER and Phyre2 web servers. The results showed that it fairly has a suitable RNA folding in terms of minimum energy. In addition, Phyre2 could model the protein with 100% confidence and 68% coverage with human protease. Secondary structure of MP contains 45% alpha helix and 8% beta strand, 31% Disordered and 3% TM helix. The estimated TM-score for final predicted MP model was 0.38±0.13 and calculated RMSD was 15.9±3.2Aº. Phyre2 investigator showed that R217, G63, K64, F27 and G58 in active site participate in the reaction with the substrate. In conclusion, predicted structure of bacterial metallopeptidase in acidic conditions has 68% coverage with human protease.
HIGHLIGHTS
Metallopeptidase is a stable protein with suitable RNA folding.
It has proper half-life for production in prokaryotic and eukaryotic systems.
The amino acids R217, G63, K64, F27 and G58 in active site participate in the reaction with the substrate.
Predicted structure of bacterial metallopeptidase has 68% coverage with human protease
