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| | ==Crystal structure of Elongation factor 2 GDP-form== | | ==Crystal structure of Elongation factor 2 GDP-form== |
| - | <StructureSection load='5h7k' size='340' side='right' caption='[[5h7k]], [[Resolution|resolution]] 1.60Å' scene=''> | + | <StructureSection load='5h7k' size='340' side='right'caption='[[5h7k]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5h7k]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H7K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5H7K FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5h7k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii_OT3 Pyrococcus horikoshii OT3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H7K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H7K 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]] 1.599Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5h7j|5h7j]], [[5h7l|5h7l]]</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fusA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=70601 Pyrococcus horikoshii])</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=5h7k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h7k OCA], [https://pdbe.org/5h7k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h7k RCSB], [https://www.ebi.ac.uk/pdbsum/5h7k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h7k ProSAT]</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=5h7k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h7k OCA], [http://pdbe.org/5h7k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h7k RCSB], [http://www.ebi.ac.uk/pdbsum/5h7k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h7k ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/EF2_PYRHO EF2_PYRHO] |
| - | Archaea and eukaryotes have ribosomal P stalks composed of anchor protein P0 and aP1 homodimers (archaea) or P1*P2 heterodimers (eukaryotes). These P stalks recruit translational GTPases to the GTPase-associated center in ribosomes to provide energy during translation. The C-terminus of the P stalk is known to selectively recognize GTPases. Here we investigated the interaction between the P stalk and elongation factor 2 by determining the structures of Pyrococcus horikoshii EF-2 (PhoEF-2) in the Apo-form, GDP-form, GMPPCP-form (GTP-form), and GMPPCP-form bound with 11 C-terminal residues of P1 (P1C11). Helical structured P1C11 binds to a hydrophobic groove between domain G and subdomain G' of PhoEF-2, where is completely different from that of aEF-1alpha in terms of both position and sequence, implying that such interaction characteristic may be requested by how GTPases perform their functions on the ribosome. Combining PhoEF-2 P1-binding assays with a structural comparison of current PhoEF-2 structures and molecular dynamics model of a P1C11-bound GDP form, the conformational changes of the P1C11-binding groove in each form suggest that in response to the translation process, the groove has three states: closed, open, and release for recruiting and releasing GTPases.
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| - | The C-terminal helix of ribosomal P stalk recognizes a hydrophobic groove of elongation factor 2 in a novel fashion.,Tanzawa T, Kato K, Girodat D, Ose T, Kumakura Y, Wieden HJ, Uchiumi T, Tanaka I, Yao M Nucleic Acids Res. 2018 Feb 20. pii: 4877024. doi: 10.1093/nar/gky115. PMID:29471537<ref>PMID:29471537</ref>
| + | ==See Also== |
| - | | + | *[[Elongation factor 3D structures|Elongation factor 3D structures]] |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 5h7k" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Pyrococcus horikoshii]] | + | [[Category: Large Structures]] |
| - | [[Category: Kato, K]] | + | [[Category: Pyrococcus horikoshii OT3]] |
| - | [[Category: Tanzawa, T]] | + | [[Category: Kato K]] |
| - | [[Category: Uchiumi, T]] | + | [[Category: Tanzawa T]] |
| - | [[Category: Yao, M]] | + | [[Category: Uchiumi T]] |
| - | [[Category: Elongation factor]]
| + | [[Category: Yao M]] |
| - | [[Category: Gtp-binding]]
| + | |
| - | [[Category: Protein biosynthesis]]
| + | |
| - | [[Category: Translation]]
| + | |
