1EIY

THE CRYSTAL STRUCTURE OF PHENYLALANYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH COGNATE TRNAPHE

1EIY の概要

• エントリーDOI: 10.2210/pdb1eiy/pdb
• 関連するPDBエントリー: 1PYS
• 分子名称: TRNA(PHE), PHENYLALANYL-TRNA SYNTHETASE (3 entities in total)
• 機能のキーワード: aminoacyl-trna synthetase, trna recognition, ligase-rna complex, ligase/rna
• 由来する生物種: Thermus thermophilus; 詳細
• 細胞内の位置: Cytoplasm: P27001 Q5SGX2 Q5SGX1
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 150514.41

構造登録者

Goldgur, Y.,Mosyak, L.,Reshetnikova, L.,Ankilova, V.,Safro, M. (登録日: 2000-02-29, 公開日: 2000-03-06, 最終更新日: 2024-02-07)

主引用文献

Goldgur, Y.,Mosyak, L.,Reshetnikova, L.,Ankilova, V.,Lavrik, O.,Khodyreva, S.,Safro, M.
The crystal structure of phenylalanyl-tRNA synthetase from thermus thermophilus complexed with cognate tRNAPhe.
Structure, 5:59-68, 1997

PubMed Abstract: In the translation of the genetic code each aminoacyl-tRNA synthetase (aaRS) must recognize its own (cognate) tRNA and attach the corresponding amino acid to the acceptor end of tRNA, discriminating all the others. The(alphabeta)2 phenylalanyl-tRNA synthetase (PheRS) is one of the most complex enzymes in the aaRS family and is characterized by anomalous charging properties. Structurally, the enzyme belongs to class II aaRSs, as its catalytic domain is built around an antiparallel beta sheet, but functionally it resembles class I as it aminoacylates the 2'OH of the terminal ribose of tRNA (class II aaRSs aminoacylate the 3'OH). With the availability of the three-dimensional structure of the complex between multisubunit PheRS and tRNAPhe, a fuller picture of the specific tRNA-aaRS interactions is beginning to emerge.

PubMed: 9016717
DOI: 10.1016/S0969-2126(97)00166-4

実験手法

X-RAY DIFFRACTION (3.3 Å)