4myt: Difference between revisions

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New page: '''Unreleased structure''' The entry 4myt is ON HOLD Authors: Guangqiao, Liu, JianShu, Dong, Weimin, Gong, Yan, Qin Description: Crystal structure of elongation factor G (EFG)
 
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'''Unreleased structure'''


The entry 4myt is ON HOLD
==Crystal structure of elongation factor G (EFG)==
<StructureSection load='4myt' size='340' side='right'caption='[[4myt]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4myt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MYT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MYT FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.505&#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></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=4myt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4myt OCA], [https://pdbe.org/4myt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4myt RCSB], [https://www.ebi.ac.uk/pdbsum/4myt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4myt ProSAT]</span></td></tr>
</table>
== Function ==
[https://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.


Authors: Guangqiao, Liu, JianShu, Dong, Weimin, Gong, Yan, Qin
==See Also==
 
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
Description: Crystal structure of elongation factor G (EFG)
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermus thermophilus]]
[[Category: Dong J]]
[[Category: Gong W]]
[[Category: Liu G]]
[[Category: Qin Y]]

Latest revision as of 14:44, 8 November 2023

Crystal structure of elongation factor G (EFG)

4myt, resolution 3.50Å

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