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|  | <SX load='3j5y' size='340' side='right' viewer='molstar' caption='[[3j5y]], [[Resolution|resolution]] 9.70Å' scene=''> |  | <SX load='3j5y' size='340' side='right' viewer='molstar' caption='[[3j5y]], [[Resolution|resolution]] 9.70Å' scene=''> | 
|  | == Structural highlights == |  | == Structural highlights == | 
| - | <table><tr><td colspan='2'>[[3j5y]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/], [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3j2k 3j2k]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J5Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J5Y FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3j5y]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3j2k 3j2k]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J5Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J5Y FirstGlance]. <br> | 
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ETF1,ERF1, RF1, SUP45L1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), GSPT1, ERF3A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 9.7Å</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=3j5y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j5y OCA], [http://pdbe.org/3j5y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3j5y RCSB], [http://www.ebi.ac.uk/pdbsum/3j5y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3j5y ProSAT]</span></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=3j5y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j5y OCA], [https://pdbe.org/3j5y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j5y RCSB], [https://www.ebi.ac.uk/pdbsum/3j5y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j5y ProSAT]</span></td></tr> | 
|  | </table> |  | </table> | 
|  | == Function == |  | == Function == | 
| - | [[http://www.uniprot.org/uniprot/ERF1_HUMAN ERF1_HUMAN]] Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA. Component of the transient SURF complex which recruits UPF1 to stalled ribosomes in the context of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons.<ref>PMID:7990965</ref> [[http://www.uniprot.org/uniprot/ERF3A_HUMAN ERF3A_HUMAN]] Involved in translation termination in response to the termination codons UAA, UAG and UGA. Stimulates the activity of ERF1. Involved in regulation of mammalian cell growth. Component of the transient SURF complex which recruits UPF1 to stalled ribosomes in the context of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons.  | + | [https://www.uniprot.org/uniprot/ERF1_HUMAN ERF1_HUMAN] Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA. Component of the transient SURF complex which recruits UPF1 to stalled ribosomes in the context of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons.<ref>PMID:7990965</ref>  | 
|  | <div style="background-color:#fffaf0;"> |  | <div style="background-color:#fffaf0;"> | 
|  | == Publication Abstract from PubMed == |  | == Publication Abstract from PubMed == | 
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|  | __TOC__ |  | __TOC__ | 
|  | </SX> |  | </SX> | 
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] | 
|  | [[Category: Large Structures]] |  | [[Category: Large Structures]] | 
|  | [[Category: Oryctolagus cuniculus]] |  | [[Category: Oryctolagus cuniculus]] | 
| - | [[Category: Frank, J]] | + | [[Category: Frank J]] | 
| - | [[Category: Georges, A des]]
 | + | [[Category: Grassucci RA]] | 
| - | [[Category: Grassucci, R A]] | + | [[Category: Hashem Y]] | 
| - | [[Category: Hashem, Y]] | + | [[Category: Hellen CUT]] | 
| - | [[Category: Hellen, C U.T]] | + | [[Category: Pestova TV]] | 
| - | [[Category: Pestova, T V]] | + | [[Category: Taylor D]] | 
| - | [[Category: Taylor, D]] | + | [[Category: Unbehaun A]] | 
| - | [[Category: Unbehaun, A]] | + | [[Category: Des Georges A]] | 
| - | [[Category: Erf1]] | + |  | 
| - | [[Category: Erf3]]
 | + |  | 
| - | [[Category: Mammalian]]
 | + |  | 
| - | [[Category: Ribosome]]
 | + |  | 
| - | [[Category: Translation termination]]
 | + |  | 
| - | [[Category: Translation-rna complex]]
 | + |  | 
| - | [[Category: Trnaleu]]
 | + |  | 
|  |   Structural highlights   Function ERF1_HUMAN Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA. Component of the transient SURF complex which recruits UPF1 to stalled ribosomes in the context of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons.[1] 
 
  Publication Abstract from PubMed Eukaryotic translation termination results from the complex functional interplay between two release factors, eRF1 and eRF3, in which GTP hydrolysis by eRF3 couples codon recognition with peptidyl-tRNA hydrolysis by eRF1. Here, we present a cryo-electron microscopy structure of pre-termination complexes associated with eRF1*eRF3*GDPNP at 9.7 -A resolution, which corresponds to the initial pre-GTP hydrolysis stage of factor attachment and stop codon recognition. It reveals the ribosomal positions of eRFs and provides insights into the mechanisms of stop codon recognition and triggering of eRF3's GTPase activity.
 Structure of the mammalian ribosomal pre-termination complex associated with eRF1*eRF3*GDPNP.,des Georges A, Hashem Y, Unbehaun A, Grassucci RA, Taylor D, Hellen CU, Pestova TV, Frank J Nucleic Acids Res. 2013 Dec 11. PMID:24335085[2]
 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
  See Also  References ↑ Frolova L, Le Goff X, Rasmussen HH, Cheperegin S, Drugeon G, Kress M, Arman I, Haenni AL, Celis JE, Philippe M, et al.. A highly conserved eukaryotic protein family possessing properties of polypeptide chain release factor. Nature. 1994 Dec 15;372(6507):701-3. PMID:7990965 doi:http://dx.doi.org/10.1038/372701a0↑ des Georges A, Hashem Y, Unbehaun A, Grassucci RA, Taylor D, Hellen CU, Pestova TV, Frank J. Structure of the mammalian ribosomal pre-termination complex associated with eRF1*eRF3*GDPNP. Nucleic Acids Res. 2013 Dec 11. PMID:24335085 doi:http://dx.doi.org/10.1093/nar/gkt1279
 
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