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1dar
From Proteopedia
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| - | [[Image:1dar.png|left|200px]] | ||
| - | < | + | ==ELONGATION FACTOR G IN COMPLEX WITH GDP== |
| - | The | + | <StructureSection load='1dar' size='340' side='right'caption='[[1dar]], [[Resolution|resolution]] 2.40Å' scene=''> |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1dar]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. 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=1DAR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DAR FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></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=1dar FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dar OCA], [https://pdbe.org/1dar PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dar RCSB], [https://www.ebi.ac.uk/pdbsum/1dar PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dar ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == Function == | ||
| + | [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/da/1dar_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/main_output.php?pdb_ID=1dar ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| - | + | ==See Also== | |
| - | + | *[[Elongation factor 3D structures|Elongation factor 3D structures]] | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | + | ||
[[Category: Elongation Factors]] | [[Category: Elongation Factors]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Thermus thermophilus]] | + | [[Category: RCSB PDB Molecule of the Month]] |
| - | [[Category: Aevarsson | + | [[Category: Thermus thermophilus HB8]] |
| - | [[Category: Al-Karadaghi | + | [[Category: Aevarsson A]] |
| - | [[Category: Garber | + | [[Category: Al-Karadaghi S]] |
| - | [[Category: Liljas | + | [[Category: Garber M]] |
| - | [[Category: Zheltonosova | + | [[Category: Liljas A]] |
| - | + | [[Category: Zheltonosova J]] | |
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
ELONGATION FACTOR G IN COMPLEX WITH GDP
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