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1eft
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(New page: 200px<br /> <applet load="1eft" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eft, resolution 2.5Å" /> '''THE CRYSTAL STRUCTUR...) |
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'''THE CRYSTAL STRUCTURE OF ELONGATION FACTOR EF-TU FROM THERMUS AQUATICUS IN THE GTP CONFORMATION'''<br /> | '''THE CRYSTAL STRUCTURE OF ELONGATION FACTOR EF-TU FROM THERMUS AQUATICUS IN THE GTP CONFORMATION'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1EFT 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 MG and GNP as [http://en.wikipedia.org/wiki/ligands ligands]. 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:// | + | 1EFT 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 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== | ||
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[[Category: elongation factor]] | [[Category: elongation factor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:42:58 2008'' |
Revision as of 13:42, 15 February 2008
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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 with and as ligands. 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
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