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[[Image:1eft.jpg|left|200px]]
[[Image:1eft.png|left|200px]]


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==Overview==
{{ABSTRACT_8069622}}
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==
==About this Structure==
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].  
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==
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: Thirup, S.]]
[[Category: Thirup, S.]]
[[Category: Elongation factor]]
[[Category: Elongation factor]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:02:44 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 26 17:13:29 2008''

Revision as of 14:13, 26 June 2008

File:1eft.png

Template:STRUCTURE 1eft

THE CRYSTAL STRUCTURE OF ELONGATION FACTOR EF-TU FROM THERMUS AQUATICUS IN THE GTP CONFORMATION


Template:ABSTRACT 8069622

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.

Page seeded by OCA on Thu Jun 26 17:13:29 2008

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