1ttt

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[[Image:1ttt.jpg|left|200px]]<br /><applet load="1ttt" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ttt.jpg|left|200px]]
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caption="1ttt, resolution 2.7&Aring;" />
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'''PHE-TRNA, ELONGATION FACTOR EF-TU:GDPNP TERNARY COMPLEX'''<br />
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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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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER'>GNP</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''PHE-TRNA, ELONGATION FACTOR EF-TU:GDPNP TERNARY COMPLEX'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1TTT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GNP:'>GNP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1TTT with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb81_1.html Elongation Factors]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TTT OCA].
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1TTT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]. The following page contains interesting information on the relation of 1TTT with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb81_1.html Elongation Factors]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TTT OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7491491 7491491]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/7491491 7491491]
[[Category: Elongation Factors]]
[[Category: Elongation Factors]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: trna]]
[[Category: trna]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:17:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:23:04 2008''

Revision as of 12:23, 20 March 2008


PDB ID 1ttt

Drag the structure with the mouse to rotate
, resolution 2.7Å
Ligands: and
Coordinates: save as pdb, mmCIF, xml



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

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