1TTT

Phe-tRNA, elongation factoR EF-TU:GDPNP ternary complex

1TTT の概要

• エントリーDOI: 10.2210/pdb1ttt/pdb
• 分子名称: TRANSFER RIBONUCLEIC ACID (YEAST, PHE), OF ELONGATION FACTOR TU (EF-TU), MAGNESIUM ION, ... (6 entities in total)
• 機能のキーワード: protein synthesis, ef-tu, trna, ribosome, 1eft, 4tna, peptide elongation ribonucleoprotein, complex (elongation factor-trna), complex (elongation factor-trna) complex, complex (elongation factor/trna)
• 由来する生物種: Thermus aquaticus
• 細胞内の位置: Cytoplasm: Q01698
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 211107.29

構造登録者

Nissen, P.,Kjeldgaard, M.,Thirup, S.,Polekhina, G.,Reshetnikova, L.,Clark, B.F.C.,Nyborg, J. (登録日: 1995-11-16, 公開日: 1996-12-23, 最終更新日: 2024-02-14)

主引用文献

Nissen, P.,Kjeldgaard, M.,Thirup, S.,Polekhina, G.,Reshetnikova, L.,Clark, B.F.,Nyborg, J.
Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog.
Science, 270:1464-1472, 1995

PubMed Abstract: The structure of the ternary complex consisting of yeast phenylalanyl-transfer RNA (Phe-tRNAPhe), Thermus aquaticus elongation factor Tu (EF-Tu), and the guanosine triphosphate (GTP) analog GDPNP was determined by x-ray crystallography at 2.7 angstrom resolution. The ternary complex participates in placing the amino acids in their correct order when messenger RNA is translated into a protein sequence on the ribosome. The EF-Tu-GDPNP component binds to one side of the acceptor helix of Phe-tRNAPhe involving all three domains of EF-Tu. Binding sites for the phenylalanylated CCA end and the phosphorylated 5' end are located at domain interfaces, whereas the T stem interacts with the surface of the beta-barrel domain 3. The binding involves many conserved residues in EF-Tu. The overall shape of the ternary complex is similar to that of the translocation factor, EF-G-GDP, and this suggests a novel mechanism involving "molecular mimicry" in the translational apparatus.

PubMed: 7491491

実験手法

X-RAY DIFFRACTION (2.7 Å)