1elo: Difference between revisions

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 ==ELONGATION FACTOR G WITHOUT NUCLEOTIDE==
-<StructureSection load='1elo' size='340' side='right' caption='[[1elo]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
+<StructureSection load='1elo' size='340' side='right'caption='[[1elo]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1elo]] is a 1 chain structure with 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=1ELO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ELO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1elo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ELO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ELO 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=1elo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1elo OCA], [http://pdbe.org/1elo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1elo RCSB], [http://www.ebi.ac.uk/pdbsum/1elo 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]] 2.8&#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=1elo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1elo OCA], [https://pdbe.org/1elo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1elo RCSB], [https://www.ebi.ac.uk/pdbsum/1elo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1elo ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/EFG_THET8 EFG_THET8]] Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
+[https://www.uniprot.org/uniprot/EFG_THET8 EFG_THET8] Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in 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/el/1elo_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/el/1elo_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 17: / Line 19: @@
 </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=1elo ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The crystal structure of Thermus thermophilus elongation factor G without guanine nucleotide was determined to 2.85 A. This GTPase has five domains with overall dimensions of 50 x 60 x 118 A. The GTP binding domain has a core common to other GTPases with a unique subdomain which probably functions as an intrinsic nucleotide exchange factor. Domains I and II are homologous to elongation factor Tu and their arrangement, both with and without GDP, is more similar to elongation factor Tu in complex with a GTP analogue than with GDP. Domains III and V show structural similarities to ribosomal proteins. Domain IV protrudes from the main body of the protein and has an extraordinary topology with a left-handed cross-over connection between two parallel beta-strands.
-Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus.,AEvarsson A, Brazhnikov E, Garber M, Zheltonosova J, Chirgadze Y, al-Karadaghi S, Svensson LA, Liljas A EMBO J. 1994 Aug 15;13(16):3669-77. PMID:8070397<ref>PMID:8070397</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1elo" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Elongation factor|Elongation factor]]
+*[[Elongation factor 3D structures|Elongation factor 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Thermus thermophilus]]
+[[Category: Large Structures]]
-[[Category: Aevarsson, A]]
+[[Category: Thermus thermophilus HB8]]
-[[Category: Al-Karadaghi, S]]
+[[Category: Aevarsson A]]
-[[Category: Brazhnikov, E]]
+[[Category: Al-Karadaghi S]]
-[[Category: Chirgadze, Yu]]
+[[Category: Brazhnikov E]]
-[[Category: Garber, M]]
+[[Category: Chirgadze Yu]]
-[[Category: Liljas, A]]
+[[Category: Garber M]]
-[[Category: Svensson, L A]]
+[[Category: Liljas A]]
-[[Category: Zheltonosova, J]]
+[[Category: Svensson LA]]
-[[Category: Elongation factor]]
+[[Category: Zheltonosova J]]
-[[Category: Gtp binding protein]]
-[[Category: Hydrolase]]
-[[Category: Ribosomal translocase]]