1ttt

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[[Image:1ttt.jpg|left|200px]]
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{{Structure
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|PDB= 1ttt |SIZE=350|CAPTION= <scene name='initialview01'>1ttt</scene>, resolution 2.7&Aring;
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{{STRUCTURE_1ttt| PDB=1ttt | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ttt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ttt OCA], [http://www.ebi.ac.uk/pdbsum/1ttt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ttt RCSB]</span>
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'''PHE-TRNA, ELONGATION FACTOR EF-TU:GDPNP TERNARY COMPLEX'''
'''PHE-TRNA, ELONGATION FACTOR EF-TU:GDPNP TERNARY COMPLEX'''
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[[Category: 1eft]]
[[Category: 1eft]]
[[Category: 4tna]]
[[Category: 4tna]]
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[[Category: complex (elongation factor/trna)]]
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[[Category: Ef-tu]]
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[[Category: ef-tu]]
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[[Category: Peptide elongation ribonucleoprotein]]
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[[Category: peptide elongation ribonucleoprotein]]
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[[Category: Protein synthesis]]
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[[Category: protein synthesis]]
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[[Category: Ribosome]]
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[[Category: ribosome]]
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[[Category: Trna]]
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[[Category: trna]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:21:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:00:57 2008''
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Revision as of 07:21, 3 May 2008

Image:1ttt.jpg

Template:STRUCTURE 1ttt

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. 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 Sat May 3 10:21:17 2008

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