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Structural Basis for the Recognition of para ‐Benzoyl‐ L ‐phenylalanine by Evolved Aminoacyl‐tRNA Synthetases
Author(s) -
Liu Wenshe,
Alfonta Lital,
Mack Antha V.,
Schultz Peter G.
Publication year - 2007
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200701990
Subject(s) - phenylalanine , chemistry , aminoacyl trna , tyrosine , aminoacyl trna synthetase , transfer rna , amino acid , hydrogen bond , stereochemistry , enzyme , biochemistry , amino acyl trna synthetases , phenylalanine hydroxylase , aromatic amino acids , molecule , organic chemistry , rna , gene
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.