1efu: Difference between revisions

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 ==ELONGATION FACTOR COMPLEX EF-TU/EF-TS FROM ESCHERICHIA COLI==
-<StructureSection load='1efu' size='340' side='right' caption='[[1efu]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+<StructureSection load='1efu' size='340' side='right'caption='[[1efu]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1efu]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. The September 2006 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Elongation Factors''  by David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2006_9 10.2210/rcsb_pdb/mom_2006_9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EFU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EFU FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1efu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The September 2006 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Elongation Factors''  by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2006_9 10.2210/rcsb_pdb/mom_2006_9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EFU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EFU FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1efu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1efu OCA], [http://pdbe.org/1efu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1efu RCSB], [http://www.ebi.ac.uk/pdbsum/1efu PDBsum]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1efu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1efu OCA], [https://pdbe.org/1efu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1efu RCSB], [https://www.ebi.ac.uk/pdbsum/1efu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1efu ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/EFTS_ECOLI EFTS_ECOLI]] 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.[HAMAP-Rule:MF_00050]
+[https://www.uniprot.org/uniprot/EFTU2_ECOLI EFTU2_ECOLI] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.[HAMAP-Rule:MF_00118]  May play an important regulatory role in cell growth and in the bacterial response to nutrient deprivation.[HAMAP-Rule:MF_00118]
 == 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/ef/1efu_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ef/1efu_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=1efu ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The crystal structure of the EF-Tu.EF-Ts complex from Escherichia coli has been determined to a resolution of 2.5 A. The complex contains two subunits of each of the elongation factors. The two EF-Ts molecules form a tight dimer, but there is little contact between the two EF-Tu molecules. The interaction of EF-Ts with EF-Tu results principally in the disruption of the Mg2+ ion binding site, thereby reducing the affinity of EF-Tu for guanine nucleotides.
-The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolution.,Kawashima T, Berthet-Colominas C, Wulff M, Cusack S, Leberman R Nature. 1996 Feb 8;379(6565):511-8. PMID:8596629<ref>PMID:8596629</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1efu" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Elongation factor|Elongation factor]]
-== References ==
+*[[Elongation factor 3D structures|Elongation factor 3D structures]]
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
 [[Category: Elongation Factors]]
+[[Category: Escherichia coli]]
+[[Category: Large Structures]]
 [[Category: RCSB PDB Molecule of the Month]]
-[[Category: Berthet-Colominas, C]]
+[[Category: Berthet-Colominas C]]
-[[Category: Cusack, S]]
+[[Category: Cusack S]]
-[[Category: Kawashima, T]]
+[[Category: Kawashima T]]
-[[Category: Leberman, R]]
+[[Category: Leberman R]]
-[[Category: Wulff, M]]
+[[Category: Wulff M]]
-[[Category: Elongation factor]]