To investigate the mechanism by which SeryltRNA synthetase (SerRS) discriminates against noncognate amino acids in forming the seryl adenylate intermediate, we used the HierDock and SCREAM computational methods to predict the binding conformation and energy for the 20 natural amino acids in the best-binding mode and in the activating mode. This shows the predicted structure of Ser in the SerRS best-binding mode. We predict that Asn will compete with Ser for formation of the activated intermediate and hence that SerRS misactivates Asn at a rate comparable to Thr (not yet tested experimentally). For further information see Fidelity of Seryl-tRNA Synthetase to Binding of Natural Amino Acids from HierDock First Principles Computations by McClendon et al., pp. 195–203.
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