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1dar

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(New page: 200px<br /> <applet load="1dar" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dar, resolution 2.4&Aring;" /> '''ELONGATION FACTOR G ...)
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[[Image:1dar.gif|left|200px]]<br />
 
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<applet load="1dar" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1dar, resolution 2.4&Aring;" />
 
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'''ELONGATION FACTOR G IN COMPLEX WITH GDP'''<br />
 
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==Overview==
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==ELONGATION FACTOR G IN COMPLEX WITH GDP==
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BACKGROUND: Elongation factor G (EF-G) catalyzes the translocation step of, translation. During translocation EF-G passes through four main, conformational states: the GDP complex, the nucleotide-free state, the GTP, complex, and the GTPase conformation. The first two of these conformations, have been previously investigated by crystallographic methods. RESULTS:, The structure of EF-G-GDP has been refined at 2.4 A resolution. Comparison, with the nucleotide-free structure reveals that, upon GDP release, the, phosphate-binding loop (P-loop) adopts a closed conformation. This affects, the position of helix CG, the switch II loop and domains II, IV and V., Asp83 has a conformation similar to the conformation of the corresponding, residue in the EF-Tu/EF-Ts complex. The magnesium ion is absent in, EF-G-GDP. CONCLUSIONS: The results illustrate that conformational changes, in the P-loop can be transmitted to other parts of the structure. A, comparison of the structures of EF-G and EF-Tu suggests that EF-G, like, EF-Tu, undergoes a transition with domain rearrangements. The conformation, of EF-G-GDP around the nucleotide-binding site may be related to the, mechanism of nucleotide exchange.
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<StructureSection load='1dar' size='340' side='right'caption='[[1dar]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<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>
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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]] 2.4&#8491;</td></tr>
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<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>
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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=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>
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</table>
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== Function ==
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[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.
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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/da/1dar_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=1dar ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1DAR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with GDP as [http://en.wikipedia.org/wiki/ligand ligand]. The following page contains interesting information on the relation of 1DAR with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb81_1.html Elongation Factors]]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DAR OCA].
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*[[Elongation factor 3D structures|Elongation factor 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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The structure of elongation factor G in complex with GDP: conformational flexibility and nucleotide exchange., al-Karadaghi S, Aevarsson A, Garber M, Zheltonosova J, Liljas A, Structure. 1996 May 15;4(5):555-65. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8736554 8736554]
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[[Category: Elongation Factors]]
[[Category: Elongation Factors]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Thermus thermophilus]]
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[[Category: RCSB PDB Molecule of the Month]]
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[[Category: Aevarsson, A.]]
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[[Category: Thermus thermophilus HB8]]
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[[Category: Al-Karadaghi, S.]]
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[[Category: Aevarsson A]]
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[[Category: Garber, M.]]
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[[Category: Al-Karadaghi S]]
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[[Category: Liljas, A.]]
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[[Category: Garber M]]
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[[Category: Zheltonosova, J.]]
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[[Category: Liljas A]]
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[[Category: GDP]]
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[[Category: Zheltonosova J]]
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[[Category: ribosomal translocase]]
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[[Category: translational gtpase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 08:58:44 2007''
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Current revision

ELONGATION FACTOR G IN COMPLEX WITH GDP

PDB ID 1dar

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