5ot7: Difference between revisions

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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'''


The entry 5ot7 is ON HOLD
==Elongation factor G-ribosome complex captures in the absence of inhibitors.==
<SX load='5ot7' size='340' side='right' viewer='molstar' caption='[[5ot7]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ot7]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [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]] 3.8&#8491;</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/RS2_THET8 RS2_THET8] Spans the head-body hinge region of the 30S subunit. Is loosely associated with the 30S subunit.[HAMAP-Rule:MF_00291_B]
<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.


Authors: Mace, K., Giudice, E., Chat, S., Gillet, R.
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>


Description: Elongation factor G-ribosome complex captures in the absence of inhibitors
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Mace, K]]
<div class="pdbe-citations 5ot7" style="background-color:#fffaf0;"></div>
[[Category: Gillet, R]]
 
[[Category: Chat, S]]
==See Also==
[[Category: Giudice, E]]
*[[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: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Thermus thermophilus HB8]]
[[Category: Chat S]]
[[Category: Gillet R]]
[[Category: Giudice E]]
[[Category: Mace K]]