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1eft

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[[Image:1eft.jpg|left|200px]]<br /><applet load="1eft" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1eft.jpg|left|200px]]
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caption="1eft, resolution 2.5&Aring;" />
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'''THE CRYSTAL STRUCTURE OF ELONGATION FACTOR EF-TU FROM THERMUS AQUATICUS IN THE GTP CONFORMATION'''<br />
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{{Structure
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|PDB= 1eft |SIZE=350|CAPTION= <scene name='initialview01'>1eft</scene>, resolution 2.5&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER'>GNP</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''THE CRYSTAL STRUCTURE OF ELONGATION FACTOR EF-TU FROM THERMUS AQUATICUS IN THE GTP CONFORMATION'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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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==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=8069622 8069622]
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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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:27:22 2008''
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''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


PDB ID 1eft

Drag the structure with the mouse to rotate
, resolution 2.5Å
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

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