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| ==Crystal structure of Elongation Factor 4 (EF4/LepA) bound to the Thermus thermophilus 70S ribosome, 50S subunit of the 70S ribosome==
| | #REDIRECT [[4w2e]] This PDB entry is obsolete and replaced by 4w2e |
| <StructureSection load='4qjs' size='340' side='right' caption='[[4qjs]], [[Resolution|resolution]] 2.90Å' scene=''>
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| == Structural highlights ==
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| <table><tr><td colspan='2'>[[4qjs]] is a 31 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=4QJS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QJS FirstGlance]. <br>
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| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qjt|4qjt]], [[4w2e|4w2e]]</td></tr>
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| <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=4qjs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qjs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qjs RCSB], [http://www.ebi.ac.uk/pdbsum/4qjs PDBsum]</span></td></tr>
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| </table>
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| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Elongation factor 4 (EF4/LepA) is a highly conserved guanosine triphosphatase translation factor. It was shown to promote back-translocation of tRNAs on posttranslocational ribosome complexes and to compete with elongation factor G for interaction with pretranslocational ribosomes, inhibiting the elongation phase of protein synthesis. Here, we report a crystal structure of EF4-guanosine diphosphate bound to the Thermus thermophilus ribosome with a P-site tRNA at 2.9 angstroms resolution. The C-terminal domain of EF4 reaches into the peptidyl transferase center and interacts with the acceptor stem of the peptidyl-tRNA in the P site. The ribosome is in an unusual state of ratcheting with the 30S subunit rotated clockwise relative to the 50S subunit, resulting in a remodeled decoding center. The structure is consistent with EF4 functioning either as a back-translocase or a ribosome sequester.
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| Ribosome structure. Crystal structure of elongation factor 4 bound to a clockwise ratcheted ribosome.,Gagnon MG, Lin J, Bulkley D, Steitz TA Science. 2014 Aug 8;345(6197):684-7. doi: 10.1126/science.1253525. PMID:25104389<ref>PMID:25104389</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| == References ==
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| <references/>
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| __TOC__
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| </StructureSection>
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| [[Category: Thermus thermophilus]]
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| [[Category: Gagnon, M G.]]
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| [[Category: Lin, J.]]
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| [[Category: Steitz, T A.]]
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| [[Category: Acylated p-site trna]]
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| [[Category: Ef4]]
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| [[Category: Elogation]]
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| [[Category: Lepa]]
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| [[Category: Ribosome]]
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| [[Category: Translation]]
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This PDB entry is obsolete and replaced by 4w2e