1zh6
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Crystal Structure of p-acetylphenylalanine-tRNA synthetase in complex with p-acetylphenylalanine
OverviewOverview
It has been recently shown that orthogonal tRNA/aminoacyl-tRNA synthetase pairs can be evolved to allow genetic incorporation of unnatural amino acids into proteins in both prokaryotes and eukaryotes. Here we describe the crystal structure of an evolved aminoacyl-tRNA synthetase that charges the unnatural amino acid p-acetylphenylalanine. Molecular recognition is due to altered hydrogen bonding and packing interactions with bound substrate that result from changes in both side-chain and backbone conformation.
About this StructureAbout this Structure
1ZH6 is a Single protein structure of sequence from Methanocaldococcus jannaschii with 4AF and BME as ligands. Active as Tyrosine--tRNA ligase, with EC number 6.1.1.1 Full crystallographic information is available from OCA.
ReferenceReference
Structural characterization of a p-acetylphenylalanyl aminoacyl-tRNA synthetase., Turner JM, Graziano J, Spraggon G, Schultz PG, J Am Chem Soc. 2005 Nov 2;127(43):14976-7. PMID:16248607
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