1ttt
From Proteopedia
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- | [[Image:1ttt.jpg|left|200px]] | + | [[Image:1ttt.jpg|left|200px]] |
- | + | ||
- | '''PHE-TRNA, ELONGATION FACTOR EF-TU:GDPNP TERNARY COMPLEX''' | + | {{Structure |
+ | |PDB= 1ttt |SIZE=350|CAPTION= <scene name='initialview01'>1ttt</scene>, resolution 2.7Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER'>GNP</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''PHE-TRNA, ELONGATION FACTOR EF-TU:GDPNP TERNARY COMPLEX''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1TTT is a [ | + | 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== | ||
- | 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:// | + | 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]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''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
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, resolution 2.7Å | |||||||
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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
Page seeded by OCA on Thu Mar 20 14:23:04 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