Structural Basis for the Recognition of para-Benzoyl-L-phenylalanine by Evolved Aminoacyl-tRNA Synthetases†
Part of this work is based on experiments conducted at the Advanced Light Source (ALS). The ALS is supported by the Director, Office of Science, Office of Basic Energy Sciences, Material Sciences Division of the US Department of Energy under Contract DE-AC03-76SF00098 at the Lawrence Berkeley National Laboratory. This work is supported by grants from the National Institutes of Health (GM62159) to P.G.S., and this is manuscript 18906 of The Scripps Research Institute.
Graphical Abstract
Nonnatural interactions: The X-ray crystal structure of a mutant aminoacyl-tRNA synthetase that selectively recognizes para-benozyl-L-phenylalanine has been solved. This structure shows that mutations to the enzyme lead to new hydrophobic binding interactions with the unnatural amino acid, and a loss of specific hydrogen-bonding interactions with tyrosine, without a significant change in the polypeptide backbone conformation.
