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[[Image:1tfe.gif|left|200px]]


{{Structure
==DIMERIZATION DOMAIN OF EF-TS FROM T. THERMOPHILUS==
|PDB= 1tfe |SIZE=350|CAPTION= <scene name='initialview01'>1tfe</scene>, resolution 1.7&Aring;
<StructureSection load='1tfe' size='340' side='right'caption='[[1tfe]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1tfe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TFE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TFE FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
|GENE= TSF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus])
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tfe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tfe OCA], [https://pdbe.org/1tfe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tfe RCSB], [https://www.ebi.ac.uk/pdbsum/1tfe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tfe ProSAT]</span></td></tr>
|DOMAIN=
</table>
|RELATEDENTRY=
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tfe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tfe OCA], [http://www.ebi.ac.uk/pdbsum/1tfe PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tfe RCSB]</span>
[https://www.uniprot.org/uniprot/EFTS_THET8 EFTS_THET8] Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
}}
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tf/1tfe_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1tfe ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Elongation factor Ts (EF-Ts) functions as a nucleotide-exchange factor by binding elongation factor Tu (EF-Tu) and accelerating the GDP dissociation from EF-Tu; thus EF-Ts promotes the transition of EF-Tu from the inactive GDP form to the active GTP form. Thermus thermophilus EF-Ts exists as a stable dimer in solution which binds two molecules of EF-Tu to form a (EF-Tu.EF-Ts)2 heterotetramer. Here we report the crystal structure of the dimerization domain of EF-Ts from T. thermophilus refined to 1.7 A resolution. A three-stranded antiparallel beta-sheet from each subunit interacts to form a beta-sandwich that serves as an extensive dimer interface tethered by a disulfide bond. This interface is distinctly different from the predominantly alpha-helical one that stabilizes the EF-Ts dimer from Escherichia coli [Kawashima, T., et al. (1996) Nature 379, 511-518]. To test whether the homodimeric form of T. thermophilus EF-Ts is necessary for catalyzing nucleotide exchange, the present structure was used to design mutational changes within the dimer interface that disrupt the T. thermophilus EF-Ts dimer but not the tertiary structure of the subunits. Surprisingly, EF-Ts monomers created in this manner failed to catalyze nucleotide exchange in EF-Tu, indicating that, in vitro. T. thermophilus EF-Ts functions only as a homodimer.


'''DIMERIZATION DOMAIN OF EF-TS FROM T. THERMOPHILUS'''
Structure and importance of the dimerization domain in elongation factor Ts from Thermus thermophilus.,Jiang Y, Nock S, Nesper M, Sprinzl M, Sigler PB Biochemistry. 1996 Aug 13;35(32):10269-78. PMID:8756682<ref>PMID:8756682</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1tfe" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
Elongation factor Ts (EF-Ts) functions as a nucleotide-exchange factor by binding elongation factor Tu (EF-Tu) and accelerating the GDP dissociation from EF-Tu; thus EF-Ts promotes the transition of EF-Tu from the inactive GDP form to the active GTP form. Thermus thermophilus EF-Ts exists as a stable dimer in solution which binds two molecules of EF-Tu to form a (EF-Tu.EF-Ts)2 heterotetramer. Here we report the crystal structure of the dimerization domain of EF-Ts from T. thermophilus refined to 1.7 A resolution. A three-stranded antiparallel beta-sheet from each subunit interacts to form a beta-sandwich that serves as an extensive dimer interface tethered by a disulfide bond. This interface is distinctly different from the predominantly alpha-helical one that stabilizes the EF-Ts dimer from Escherichia coli [Kawashima, T., et al. (1996) Nature 379, 511-518]. To test whether the homodimeric form of T. thermophilus EF-Ts is necessary for catalyzing nucleotide exchange, the present structure was used to design mutational changes within the dimer interface that disrupt the T. thermophilus EF-Ts dimer but not the tertiary structure of the subunits. Surprisingly, EF-Ts monomers created in this manner failed to catalyze nucleotide exchange in EF-Tu, indicating that, in vitro. T. thermophilus EF-Ts functions only as a homodimer.
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
 
== References ==
==About this Structure==
<references/>
1TFE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TFE OCA].
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
Structure and importance of the dimerization domain in elongation factor Ts from Thermus thermophilus., Jiang Y, Nock S, Nesper M, Sprinzl M, Sigler PB, Biochemistry. 1996 Aug 13;35(32):10269-78. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8756682 8756682]
[[Category: Single protein]]
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
[[Category: Jiang, Y.]]
[[Category: Jiang Y]]
[[Category: Nesper, M.]]
[[Category: Nesper M]]
[[Category: Nock, S.]]
[[Category: Nock S]]
[[Category: Sigler, P B.]]
[[Category: Sigler PB]]
[[Category: Sprinzl, M.]]
[[Category: Sprinzl M]]
[[Category: elongation factor]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:55:17 2008''

Latest revision as of 07:37, 23 October 2024

DIMERIZATION DOMAIN OF EF-TS FROM T. THERMOPHILUS

1tfe, resolution 1.70Å

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