3vmf
From Proteopedia
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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 [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VMF FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tuf, APE_1844 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272557 Aeropyrum pernix K1]), prf1, APE_1988.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272557 Aeropyrum pernix K1])</td></tr> | ||
| + | <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=3vmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vmf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vmf RCSB], [http://www.ebi.ac.uk/pdbsum/3vmf PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <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> | |
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
[[Category: Aeropyrum pernix k1]] | [[Category: Aeropyrum pernix k1]] | ||
| - | [[Category: Ishitani, R | + | [[Category: Ishitani, R]] |
| - | [[Category: Ito, K | + | [[Category: Ito, K]] |
| - | [[Category: Kobayashi, K | + | [[Category: Kobayashi, K]] |
| - | [[Category: Nureki, O | + | [[Category: Nureki, O]] |
| - | [[Category: Saito, K | + | [[Category: Saito, K]] |
[[Category: Translation]] | [[Category: Translation]] | ||
[[Category: Translation termination]] | [[Category: Translation termination]] | ||
Revision as of 07:23, 21 December 2014
Archaeal protein
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