1ZH0

Crystal Structure of L-3-(2-napthyl)alanine-tRNA synthetase in complex with L-3-(2-napthyl)alanine

1ZH0 の概要

• エントリーDOI: 10.2210/pdb1zh0/pdb
• 関連するPDBエントリー: 1ZH6
• 分子名称: Tyrosyl-tRNA synthetase, BETA-(2-NAPHTHYL)-ALANINE, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total)
• 機能のキーワード: structural plasticity, unnatural amino acid, trna synthetase, npala, ligase
• 由来する生物種: Methanocaldococcus jannaschii
• 細胞内の位置: Cytoplasm: Q57834
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36402.27

構造登録者

Turner, J.M.,Graziano, J.,Spraggon, G.,Schultz, P.G. (登録日: 2005-04-22, 公開日: 2006-04-04, 最終更新日: 2024-02-14)

主引用文献

Turner, J.M.,Graziano, J.,Spraggon, G.,Schultz, P.G.
Structural plasticity of an aminoacyl-tRNA synthetase active site
Proc.Natl.Acad.Sci.Usa, 103:6483-6488, 2006

PubMed Abstract: Recently, tRNA aminoacyl-tRNA synthetase pairs have been evolved that allow one to genetically encode a large array of unnatural amino acids in both prokaryotic and eukaryotic organisms. We have determined the crystal structures of two substrate-bound Methanococcus jannaschii tyrosyl aminoacyl-tRNA synthetases that charge the unnatural amino acids p-bromophenylalanine and 3-(2-naphthyl)alanine (NpAla). A comparison of these structures with the substrate-bound WT synthetase, as well as a mutant synthetase that charges p-acetylphenylalanine, shows that altered specificity is due to both side-chain and backbone rearrangements within the active site that modify hydrogen bonds and packing interactions with substrate, as well as disrupt the alpha8-helix, which spans the WT active site. The high degree of structural plasticity that is observed in these aminoacyl-tRNA synthetases is rarely found in other mutant enzymes with altered specificities and provides an explanation for the surprising adaptability of the genetic code to novel amino acids.

PubMed: 16618920
DOI: 10.1073/pnas.0601756103

実験手法

X-RAY DIFFRACTION (1.9 Å)