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5ot7
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 5ot7 is ON HOLD Authors: Mace, K., Giudice, E., Chat, S., Gillet, R. Description: Elongation factor G-ribosome complex captures in the absence of i...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Elongation factor G-ribosome complex captures in the absence of inhibitors.== | |
| + | <SX load='5ot7' size='340' side='right' viewer='molstar' caption='[[5ot7]], [[Resolution|resolution]] 3.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5ot7]] is a 10 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=5OT7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OT7 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.8Å</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>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5ot7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ot7 OCA], [https://pdbe.org/5ot7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ot7 RCSB], [https://www.ebi.ac.uk/pdbsum/5ot7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ot7 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/RS16_THET8 RS16_THET8] Binds to the lower part of the body of the 30S subunit, where it stabilizes two of its domains.[HAMAP-Rule:MF_00385] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | During translation's elongation cycle, elongation factor G (EF-G) promotes messenger and transfer RNA translocation through the ribosome. Until now, the structures reported for EF-G-ribosome complexes have been obtained by trapping EF-G in the ribosome. These results were based on use of non-hydrolyzable guanosine 5'-triphosphate (GTP) analogs, specific inhibitors or a mutated EF-G form. Here, we present the first cryo-electron microscopy structure of EF-G bound to ribosome in the absence of an inhibitor. The structure reveals a natural conformation of EF-G.GDP in the ribosome, with a previously unseen conformation of its third domain. These data show how EF-G must affect translocation, and suggest the molecular mechanism by which fusidic acid antibiotic prevents the release of EF-G after GTP hydrolysis. | ||
| - | + | The structure of an elongation factor G-ribosome complex captured in the absence of inhibitors.,Mace K, Giudice E, Chat S, Gillet R Nucleic Acids Res. 2018 Feb 2. pii: 4835058. doi: 10.1093/nar/gky081. PMID:29408956<ref>PMID:29408956</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5ot7" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | |
| - | [[Category: | + | ==See Also== |
| - | [[Category: Giudice | + | *[[Elongation factor 3D structures|Elongation factor 3D structures]] |
| + | *[[Ribosomal protein THX 3D structures|Ribosomal protein THX 3D structures]] | ||
| + | *[[Ribosome 3D structures|Ribosome 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </SX> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Thermus thermophilus HB8]] | ||
| + | [[Category: Chat S]] | ||
| + | [[Category: Gillet R]] | ||
| + | [[Category: Giudice E]] | ||
| + | [[Category: Mace K]] | ||
Current revision
Elongation factor G-ribosome complex captures in the absence of inhibitors.
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