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1eft
From Proteopedia
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|PDB= 1eft |SIZE=350|CAPTION= <scene name='initialview01'>1eft</scene>, resolution 2.5Å | |PDB= 1eft |SIZE=350|CAPTION= <scene name='initialview01'>1eft</scene>, resolution 2.5Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1eft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eft OCA], [http://www.ebi.ac.uk/pdbsum/1eft PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1eft RCSB]</span> | ||
}} | }} | ||
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[[Category: Nyborg, J.]] | [[Category: Nyborg, J.]] | ||
[[Category: Thirup, S.]] | [[Category: Thirup, S.]] | ||
| - | [[Category: GNP]] | ||
| - | [[Category: MG]] | ||
[[Category: elongation factor]] | [[Category: elongation factor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:01:42 2008'' |
Revision as of 17:01, 30 March 2008
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| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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 Sun Mar 30 20:01:42 2008
