1ttt
From Proteopedia
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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 and 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 Thu Feb 21 15:17:19 2008
Categories: Elongation Factors | Single protein | Thermus aquaticus | Clark, B F.C. | Kjeldgaard, M. | Nissen, P. | Nyborg, J. | Polekhina, G. | Reshetnikova, L. | Thirup, S. | GNP | MG | 1eft | 4tna | Complex (elongation factor/trna) | Ef-tu | Peptide elongation ribonucleoprotein | Protein synthesis | Ribosome | Trna
