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

doi:10.1002/anie.200701990

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 journal › Article › peer-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 language	English
Pages (from-to)	6073-6075
Number of pages	3
Journal	Angewandte Chemie - International Edition
Volume	46
Issue number	32
DOIs	https://doi.org/10.1002/anie.200701990
State	Published - 27 Aug 2007
Externally published	Yes

Keywords

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

ASJC Scopus subject areas

Catalysis
Chemistry (all)

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10.1002/anie.200701990

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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.",

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AU - Alfonta, Lital

AU - Mack, Antha V.

AU - Schultz, Peter G.

PY - 2007/8/27

Y1 - 2007/8/27

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AB - (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.

KW - Amino acids

KW - Enzymes

KW - Hydrophobic interactions

KW - Photo-cross-linker

KW - Protein structures

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

Abstract

Keywords

ASJC Scopus subject areas

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