3e1y

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{{Seed}}
 
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[[Image:3e1y.jpg|left|200px]]
 
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==Crystal structure of human eRF1/eRF3 complex==
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The line below this paragraph, containing "STRUCTURE_3e1y", creates the "Structure Box" on the page.
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<StructureSection load='3e1y' size='340' side='right'caption='[[3e1y]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3e1y]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E1Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E1Y FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr>
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{{STRUCTURE_3e1y| PDB=3e1y | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3e1y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e1y OCA], [https://pdbe.org/3e1y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e1y RCSB], [https://www.ebi.ac.uk/pdbsum/3e1y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e1y ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e1/3e1y_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3e1y ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Eukaryotic translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act cooperatively to ensure efficient stop codon recognition and fast polypeptide release. The crystal structures of human and Schizosaccharomyces pombe full-length eRF1 in complex with eRF3 lacking the GTPase domain revealed details of the interaction between these two factors and marked conformational changes in eRF1 that occur upon binding to eRF3, leading eRF1 to resemble a tRNA molecule. Small-angle X-ray scattering analysis of the eRF1/eRF3/GTP complex suggested that eRF1's M domain contacts eRF3's GTPase domain. Consistently, mutation of Arg192, which is predicted to come in close contact with the switch regions of eRF3, revealed its important role for eRF1's stimulatory effect on eRF3's GTPase activity. An ATP molecule used as a crystallization additive was bound in eRF1's putative decoding area. Mutational analysis of the ATP-binding site shed light on the mechanism of stop codon recognition by eRF1.
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===Crystal structure of human eRF1/eRF3 complex===
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Structural insights into eRF3 and stop codon recognition by eRF1.,Cheng Z, Saito K, Pisarev AV, Wada M, Pisareva VP, Pestova TV, Gajda M, Round A, Kong C, Lim M, Nakamura Y, Svergun DI, Ito K, Song H Genes Dev. 2009 May 1;23(9):1106-18. PMID:19417105<ref>PMID:19417105</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The line below this paragraph, {{ABSTRACT_PUBMED_19417105}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3e1y" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 19417105 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19417105}}
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__TOC__
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</StructureSection>
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==About this Structure==
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3E1Y is a 8 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E1Y OCA].
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==Reference==
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<ref group="xtra">PMID:19417105</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Cheng, Z.]]
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[[Category: Large Structures]]
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[[Category: Kong, C.]]
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[[Category: Cheng Z]]
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[[Category: Lim, M.]]
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[[Category: Kong C]]
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[[Category: Song, H.]]
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[[Category: Lim M]]
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[[Category: Acetylation]]
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[[Category: Song H]]
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[[Category: Cytoplasm]]
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[[Category: Erf1]]
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[[Category: Erf3]]
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[[Category: Gtp-binding]]
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[[Category: Nucleotide-binding]]
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[[Category: Peptide release]]
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[[Category: Protein biosynthesis]]
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[[Category: Ptc]]
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[[Category: Translation termination]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 20 17:06:06 2009''
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Current revision

Crystal structure of human eRF1/eRF3 complex

PDB ID 3e1y

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