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1tfe

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[[Image:1tfe.gif|left|200px]]
 
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{{Structure
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==DIMERIZATION DOMAIN OF EF-TS FROM T. THERMOPHILUS==
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|PDB= 1tfe |SIZE=350|CAPTION= <scene name='initialview01'>1tfe</scene>, resolution 1.7&Aring;
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<StructureSection load='1tfe' size='340' side='right'caption='[[1tfe]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<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>
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|ACTIVITY=
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</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>
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|GENE= TSF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus])
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<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>
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}}
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tf/1tfe_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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'''DIMERIZATION DOMAIN OF EF-TS FROM T. THERMOPHILUS'''
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==See Also==
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*[[Elongation factor 3D structures|Elongation factor 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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[[Category: Large Structures]]
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==About this Structure==
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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].
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==Reference==
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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]
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[[Category: Single protein]]
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[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
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[[Category: Jiang, Y.]]
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[[Category: Jiang Y]]
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[[Category: Nesper, M.]]
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[[Category: Nesper M]]
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[[Category: Nock, S.]]
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[[Category: Nock S]]
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[[Category: Sigler, P B.]]
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[[Category: Sigler PB]]
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[[Category: Sprinzl, M.]]
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[[Category: Sprinzl M]]
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[[Category: elongation factor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:17:41 2008''
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Current revision

DIMERIZATION DOMAIN OF EF-TS FROM T. THERMOPHILUS

PDB ID 1tfe

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