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1eft
From Proteopedia
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| - | [[Image:1eft.jpg|left|200px]] | + | [[Image:1eft.jpg|left|200px]] |
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| - | '''THE CRYSTAL STRUCTURE OF ELONGATION FACTOR EF-TU FROM THERMUS AQUATICUS IN THE GTP CONFORMATION''' | + | {{Structure |
| + | |PDB= 1eft |SIZE=350|CAPTION= <scene name='initialview01'>1eft</scene>, resolution 2.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER'>GNP</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''THE CRYSTAL STRUCTURE OF ELONGATION FACTOR EF-TU FROM THERMUS AQUATICUS IN THE GTP CONFORMATION''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1EFT is a [ | + | 1EFT 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 1EFT 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=1EFT OCA]. |
==Reference== | ==Reference== | ||
| - | The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation., Kjeldgaard M, Nissen P, Thirup S, Nyborg J, Structure. 1993 Sep 15;1(1):35-50. PMID:[http:// | + | The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation., Kjeldgaard M, Nissen P, Thirup S, Nyborg J, Structure. 1993 Sep 15;1(1):35-50. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8069622 8069622] |
[[Category: Elongation Factors]] | [[Category: Elongation Factors]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: elongation factor]] | [[Category: elongation factor]] | ||
| - | ''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 10:55:10 2008'' |
Revision as of 08:55, 20 March 2008
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| , resolution 2.5Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE CRYSTAL STRUCTURE OF ELONGATION FACTOR EF-TU FROM THERMUS AQUATICUS IN THE GTP CONFORMATION
Overview
BACKGROUND: Elongation factor Tu (EF-Tu) is a GTP-binding protein that is crucial for protein biosynthesis. In the GTP form of the molecule, EF-Tu binds tightly to aminoacyl-tRNA, forming a ternary complex that interacts with the ribosomal acceptor site. During this interaction, GTP is hydrolyzed, and EF-Tu.GDP is ejected. RESULTS: The crystal structure of EF-Tu from Thermus aquaticus, complexed to the GTP analogue GDPNP, has been determined at 2.5 A resolution and compared to the structure of Escherichia coli EF-Tu.GDP. During the transition from the GDP (inactive) to the GTP (active) form, domain 1, containing the GTP-binding site, undergoes internal conformational changes similar to those observed in ras-p21. In addition, a dramatic rearrangement of domains is observed, corresponding to a rotation of 90.8 degrees of domain 1 relative to domains 2 and 3. Residues that are affected in the binding of aminoacyl-tRNA are found in or near the cleft formed by the domain interface. CONCLUSION: GTP binding by EF-Tu leads to dramatic conformational changes which expose the tRNA binding site. It appears that tRNA binding to EF-Tu induces a further conformational change, which may affect the GTPase activity.
About this Structure
1EFT is a Single protein structure of sequence from Thermus aquaticus. The following page contains interesting information on the relation of 1EFT with [Elongation Factors]. Full crystallographic information is available from OCA.
Reference
The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation., Kjeldgaard M, Nissen P, Thirup S, Nyborg J, Structure. 1993 Sep 15;1(1):35-50. PMID:8069622
Page seeded by OCA on Thu Mar 20 10:55:10 2008
