1ZH6

Crystal Structure of p-acetylphenylalanine-tRNA synthetase in complex with p-acetylphenylalanine

Summary for 1ZH6

Entry DOI	10.2210/pdb1zh6/pdb
Related	1ZH0
Descriptor	Tyrosyl-tRNA synthetase, 4-ACETYL-L-PHENYLALANINE, BETA-MERCAPTOETHANOL, ... (4 entities in total)
Functional Keywords	structural plasticity, unnatural amino acid, trna synthetase, ketone, ligase
Biological source	Methanocaldococcus jannaschii
Cellular location	Cytoplasm: Q57834
Total number of polymer chains	1
Total formula weight	36463.41
Authors	Turner, J.M.,Graziano, J.,Spraggon, G.,Schultz, P.G. (deposition date: 2005-04-22, release date: 2006-04-04, Last modification date: 2023-11-15)
Primary citation	Turner, J.M.,Graziano, J.,Spraggon, G.,Schultz, P.G. Structural characterization of a p-acetylphenylalanyl aminoacyl-tRNA synthetase. J.Am.Chem.Soc., 127:14976-14977, 2005 Cited by PubMed Abstract: 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. PubMed: 16248607 DOI: 10.1021/ja0549042 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.5 Å)

Structure validation