From Proteopedia

---

Revision as of 06:59, 18 November 2007

proteopedia linkproteopedia link

spinqualitylabelsall models 1ttt, resolution 2.7Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

PHE-TRNA, ELONGATION FACTOR EF-TU:GDPNP TERNARY COMPLEX

Overview

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.

About this Structure

1TTT is a Single protein structure of sequence from Thermus aquaticus with MG and GNP as ligands. The following page contains interesting information on the relation of 1TTT with [Elongation Factors]. Full crystallographic information is available from OCA.

Reference

Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog., Nissen P, Kjeldgaard M, Thirup S, Polekhina G, Reshetnikova L, Clark BF, Nyborg J, Science. 1995 Dec 1;270(5241):1464-72. PMID:7491491

Page seeded by OCA on Sun Nov 18 09:06:41 2007