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

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. 2007 Wiley-VCH Verlag GmbH & Co. KGaA.

authors

• Liu, Wenshe

published proceedings

• Angew Chem Int Ed Engl

author list (cited authors)

• Liu, W., Alfonta, L., Mack, A. V., & Schultz, P. G.

citation count

• 24

complete list of authors

• Liu, Wenshe||Alfonta, Lital||Mack, Antha V||Schultz, Peter G

publication date

• August 2007

publisher

• Wiley  Publisher

published in

• Angewandte Chemie International Edition  Journal

keywords

• Amino Acyl-trna Synthetases
• Benzophenones
• Binding Sites
• Crystallography, X-Ray
• Directed Molecular Evolution
• Molecular Structure
• Mutagenesis
• Phenylalanine
• Protein Binding

Digital Object Identifier (DOI)

• 10.1002/anie.200701990

start page

• 6073

end page

• 6075

volume

• 46

issue

• 32

URL

• http%3A%2F%2Fdx.doi.org%2F10.1002%2Fanie.200701990