3vmf: Difference between revisions
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==Archaeal protein== | |||
<StructureSection load='3vmf' size='340' side='right'caption='[[3vmf]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3vmf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aeropyrum_pernix_K1 Aeropyrum pernix K1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VMF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VMF 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]] 2.3Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3vmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vmf OCA], [https://pdbe.org/3vmf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vmf RCSB], [https://www.ebi.ac.uk/pdbsum/3vmf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vmf ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/EF1A_AERPE EF1A_AERPE] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis (By similarity). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
When a stop codon appears at the ribosomal A site, the class I and II release factors (RFs) terminate translation. In eukaryotes and archaea, the class I and II RFs form a heterodimeric complex, and complete the overall translation termination process in a GTP-dependent manner. However, the structural mechanism of the translation termination by the class I and II RF complex remains unresolved. In archaea, archaeal elongation factor 1 alpha (aEF1alpha), a carrier GTPase for tRNA, acts as a class II RF by forming a heterodimeric complex with archaeal RF1 (aRF1). We report the crystal structure of the aRF1.aEF1alpha complex, the first active class I and II RF complex. This structure remarkably resembles the tRNA.EF-Tu complex, suggesting that aRF1 is efficiently delivered to the ribosomal A site, by mimicking tRNA. It provides insights into the mechanism that couples GTP hydrolysis by the class II RF to stop codon recognition and peptidyl-tRNA hydrolysis by the class I RF. We discuss the different mechanisms by which aEF1alpha recognizes aRF1 and aPelota, another aRF1-related protein and molecular evolution of the three functions of aEF1alpha. | |||
Structural basis for translation termination by archaeal RF1 and GTP-bound EF1alpha complex.,Kobayashi K, Saito K, Ishitani R, Ito K, Nureki O Nucleic Acids Res. 2012 Jul 5. PMID:22772989<ref>PMID:22772989</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3vmf" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Elongation factor 3D structures|Elongation factor 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Aeropyrum pernix K1]] | |||
[[Category: Large Structures]] | |||
[[Category: Ishitani R]] | |||
[[Category: Ito K]] | |||
[[Category: Kobayashi K]] | |||
[[Category: Nureki O]] | |||
[[Category: Saito K]] | |||
