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4myu
From Proteopedia
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==Crystal structure of elongation factor G mutant(EFG)== | ==Crystal structure of elongation factor G mutant(EFG)== | ||
<StructureSection load='4myu' size='340' side='right' caption='[[4myu]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='4myu' size='340' side='right' caption='[[4myu]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
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</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>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </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>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4myt|4myt]], [[4m1k|4m1k]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4myt|4myt]], [[4m1k|4m1k]]</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=4myu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4myu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4myu RCSB], [http://www.ebi.ac.uk/pdbsum/4myu PDBsum]</span></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=4myu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4myu OCA], [http://pdbe.org/4myu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4myu RCSB], [http://www.ebi.ac.uk/pdbsum/4myu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4myu 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. | [[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. | ||
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| + | ==See Also== | ||
| + | *[[Elongation factor|Elongation factor]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 08:20, 4 August 2016
Crystal structure of elongation factor G mutant(EFG)
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Categories: Dong, J | Gong, W | Liu, G | Qin, Y | Efg | Elongation factor g | Translation
