Structural Basis for the Recognition of  para ‐Benzoyl‐ L ‐phenylalanine by Evolved Aminoacyl‐tRNA Synthetases | Zendy

Liu Wenshe | Zendy; Alfonta Lital | Zendy; Mack Antha V. | Zendy; Schultz Peter G. | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Premium

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.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here

Accelerating Research