Structural basis for the recognition of para-benzoyl-L-phenylalanine by evolved aminoacyl-tRNA synthetases

Wenshe Liu, Lital Alfonta, Antha V. Mack, Peter G. Schultz

Research output: Contribution to journalArticlepeer-review

21 Scopus citations

Abstract

(Chemical Equation Presented) 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.

Original languageEnglish
Pages (from-to)6073-6075
Number of pages3
JournalAngewandte Chemie - International Edition
Volume46
Issue number32
DOIs
StatePublished - 27 Aug 2007
Externally publishedYes

Keywords

  • Amino acids
  • Enzymes
  • Hydrophobic interactions
  • Photo-cross-linker
  • Protein structures

ASJC Scopus subject areas

  • Catalysis
  • Chemistry (all)

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