Molecular basis of ligand recognition by OASS from E. histolytica: Insights from structural and molecular dynamics simulation studies

• Published in: Biochimica et biophysica acta Vol. 1830; no. 10; pp. 4573 - 4583
• Main Authors: Raj, Isha, Mazumder, Mohit, Gourinath, Samudrala
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.10.2013
• Subjects: Active site cleft; active sites; biochemical pathways; Conformational change; Crystallography, X-Ray; cysteine; Cysteine biosynthetic pathway; Cysteine Synthase - chemistry; Cysteine Synthase - metabolism; energy; Entamoeba histolytica; Entamoeba histolytica - enzymology; Inhibition; isoleucine; Ligand binding; Ligands; lysine; methionine; Models, Molecular; molecular dynamics; Molecular Dynamics Simulation; nitrogen; O-acetyl serine sulfhydrylase; pyridoxal phosphate; schiff bases; X-ray diffraction; Ligand binding; Cysteine biosynthetic pathway; Inhibition; Conformational change; O-acetyl serine sulfhydrylase; Active site cleft

O-acetyl serine sulfhydrylase (OASS) is a pyridoxal phosphate (PLP) dependent enzyme catalyzing the last step of the cysteine biosynthetic pathway. Here we analyze and investigate the factors responsible for recognition and different conformational changes accompanying the binding of various ligands...