1B23

E. coli cysteinyl-tRNA and T. aquaticus elongation factor EF-TU:GTP ternary complex

1B23 の概要

• エントリーDOI: 10.2210/pdb1b23/pdb
• 分子名称: CYSTEINYL TRNA, ELONGATION FACTOR TU, MAGNESIUM ION, ... (7 entities in total)
• 機能のキーワード: translation elongation factor, transfer rna, protein synthesis, gene regulation-rna complex, gene regulation/rna
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 69578.83

構造登録者

Nissen, P.,Kjeldgaard, M.,Thirup, S.,Nyborg, J. (登録日: 1998-12-04, 公開日: 1998-12-07, 最終更新日: 2023-08-09)

主引用文献

Nissen, P.,Thirup, S.,Kjeldgaard, M.,Nyborg, J.
The crystal structure of Cys-tRNACys-EF-Tu-GDPNP reveals general and specific features in the ternary complex and in tRNA.
Structure Fold.Des., 7:143-156, 1999

PubMed Abstract: . The translation elongation factor EF-Tu in its GTP-bound state forms a ternary complex with any aminoacylated tRNA (aa-tRNA), except initiator tRNA and selenocysteinyl-tRNA. This complex delivers aa-tRNA to the ribosomal A site during the elongation cycle of translation. The crystal structure of the yeast Phe-tRNAPhe ternary complex with Thermus aquaticus EF-Tu-GDPNP (Phe-TC) has previously been determined as one representative of this general yet highly discriminating complex formation.

PubMed: 10368282
DOI: 10.1016/S0969-2126(99)80021-5

実験手法

X-RAY DIFFRACTION (2.6 Å)