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| | ==TRANSLATIONAL ELONGATION FACTOR G COMPLEXED WITH GDP== | | ==TRANSLATIONAL ELONGATION FACTOR G COMPLEXED WITH GDP== |
| - | <StructureSection load='2efg' size='340' side='right' caption='[[2efg]], [[Resolution|resolution]] 2.60Å' scene=''> | + | <StructureSection load='2efg' size='340' side='right'caption='[[2efg]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2efg]] is a 2 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=2EFG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EFG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2efg]] is a 2 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=2EFG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EFG FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></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]] 2.6Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2efg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2efg OCA], [http://pdbe.org/2efg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2efg RCSB], [http://www.ebi.ac.uk/pdbsum/2efg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2efg ProSAT]</span></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=2efg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2efg OCA], [https://pdbe.org/2efg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2efg RCSB], [https://www.ebi.ac.uk/pdbsum/2efg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2efg ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/EFG_THETH EFG_THETH]] 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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Elongation factor|Elongation factor]] | + | *[[Elongation factor 3D structures|Elongation factor 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Thermus thermophilus]] | + | [[Category: Large Structures]] |
| - | [[Category: Czworkowski, J]] | + | [[Category: Thermus thermophilus HB8]] |
| - | [[Category: Moore, P B]] | + | [[Category: Czworkowski J]] |
| - | [[Category: Steitz, T A]] | + | [[Category: Moore PB]] |
| - | [[Category: Wang, J]] | + | [[Category: Steitz TA]] |
| - | [[Category: Elongation]]
| + | [[Category: Wang J]] |
| - | [[Category: Elongation factor]]
| + | |
| - | [[Category: Gtp binding]]
| + | |
| - | [[Category: Gtpase]]
| + | |
| - | [[Category: Guanosine nucleotide binding]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Protein synt factor]]
| + | |
| - | [[Category: Ribosome]]
| + | |
| - | [[Category: Translation]]
| + | |
| - | [[Category: Translocase]]
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| Structural highlights
Function
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
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Elongation factor G (EF-G) catalyzes the translocation step of protein synthesis in bacteria, and like the other bacterial elongation factor, EF-Tu--whose structure is already known--it is a member of the GTPase superfamily. We have determined the crystal structure of EF-G--GDP from Thermus thermophilus. It is an elongated molecule whose large, N-terminal domain resembles the G domain of EF-Tu, except for a 90 residue insert, which covers a surface that is involved in nucleotide exchange in EF-Tu and other G proteins. The tertiary structures of the second domains of EF-G and EF-Tu are nearly identical, but the relative placement of the first two domains in EF-G--GDP resembles that seen in EF-Tu--GTP, not EF-Tu--GDP. The remaining three domains of EF-G look like RNA binding domains, and have no counterparts in EF-Tu.
The crystal structure of elongation factor G complexed with GDP, at 2.7 A resolution.,Czworkowski J, Wang J, Steitz TA, Moore PB EMBO J. 1994 Aug 15;13(16):3661-8. PMID:8070396[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Czworkowski J, Wang J, Steitz TA, Moore PB. The crystal structure of elongation factor G complexed with GDP, at 2.7 A resolution. EMBO J. 1994 Aug 15;13(16):3661-8. PMID:8070396
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