Computational Analysis of the Domain Architecture and Substrate-Gating Mechanism of Prolyl Oligopeptidases from Shewanella woodyi and Identification of Probable Lead Molecules

摘要: Prolyl oligopeptidases (POP) are serine proteases found in prokaryotes and eukaryotes which hydrolyze the peptide bond containing proline. The current study focuses on analysis of POP sequences, their distribution domain architecture Shewanella woodyi, a Gram negative, luminous bacterium causes celiac sprue similar infections marine organisms. undergoes huge inter-domain movement, allows possible route for entry any substrate. Hence, it offers an opportunity to understand mechanism substrate gating by studying possibility identify probable drug target. In present study, sequence was retrieved from GenBank data base best homologous templates were identified PSI-BLAST search. three dimensional structures closed open forms not available native form, generated homology modeling. ideal lead molecules screened computer aided virtual screening binding potential leads towards target studied molecular docking. revealed that, has propeller consist β-sheets, surrounded α-helices α/β hydrolase with catalytic triad Ser-564, Asp-646 His-681. hypothetical models showed backbone RMSD value 0.56 A 0.65 respectively. Ramachandran plot conformations accounts 99.4% 98.7% residues favoured region Our comes as insert between N-terminal C-terminal domain. Molecular docking, likeliness properties ADME prediction suggested that KUC-103481N Pramiracetum can be used woodyi.