Principal Component Analysis to Explore Transition Pathway of the Conformational Change in E. Faecalis Prolyl-tRNA Synthetase upon Substrate Binding
Strom, Alexander M.
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Aminoacyl-tRNA synthetases (AARSs) catalyze the esterification of transfer RNAs with their cognate amino acids. These multi-domain enzymes undergo conformational changes upon substrate binding. To understand the molecular mechanism of the population-shift from substrate-free conformations to bound conformation(s), the purpose of this study was to analyze the substrate-bound and substrate-free conformations of E. Faecalis Prolyl-tRNA Synthetase (ProRS) by performing Principal Component Analysis (PCA) of the molecular dynamic simulation trajectories.
E. Faecalis prolyl-tRNA Synthetase (ProRS)
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