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| | <StructureSection load='1r5n' size='340' side='right'caption='[[1r5n]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='1r5n' size='340' side='right'caption='[[1r5n]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1r5n]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_356 Cbs 356]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R5N OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1R5N FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1r5n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R5N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R5N FirstGlance]. <br> |
| - | </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></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1r5b|1r5b]], [[1r5o|1r5o]]</div></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></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sup35 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4896 CBS 356])</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=1r5n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r5n OCA], [https://pdbe.org/1r5n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r5n RCSB], [https://www.ebi.ac.uk/pdbsum/1r5n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r5n ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1r5n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r5n OCA], [http://pdbe.org/1r5n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r5n RCSB], [http://www.ebi.ac.uk/pdbsum/1r5n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1r5n ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ERF3_SCHPO ERF3_SCHPO]] Involved in translation termination. Stimulates the activity of ERF1. Binds guanine nucleotides. | + | [https://www.uniprot.org/uniprot/ERF3_SCHPO ERF3_SCHPO] Involved in translation termination. Stimulates the activity of ERF1. Binds guanine nucleotides. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cbs 356]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kong, C]] | + | [[Category: Schizosaccharomyces pombe]] |
| - | [[Category: Song, H]] | + | [[Category: Kong C]] |
| - | [[Category: Gtpase]] | + | [[Category: Song H]] |
| - | [[Category: Peptide release]]
| + | |
| - | [[Category: Translation]]
| + | |
| - | [[Category: Translation termination]]
| + | |
| Structural highlights
Function
ERF3_SCHPO Involved in translation termination. Stimulates the activity of ERF1. Binds guanine nucleotides.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Translation termination in eukaryotes is governed by two interacting release factors, eRF1 and eRF3. The crystal structure of the eEF1alpha-like region of eRF3 from S. pombe determined in three states (free protein, GDP-, and GTP-bound forms) reveals an overall structure that is similar to EF-Tu, although with quite different domain arrangements. In contrast to EF-Tu, GDP/GTP binding to eRF3c does not induce dramatic conformational changes, and Mg(2+) is not required for GDP binding to eRF3c. Mg(2+) at higher concentration accelerates GDP release, suggesting a novel mechanism for nucleotide exchange on eRF3 from that of other GTPases. Mapping sequence conservation onto the molecular surface, combined with mutagenesis analysis, identified the eRF1 binding region, and revealed an essential function for the C terminus of eRF3. The N-terminal extension, rich in acidic amino acids, blocks the proposed eRF1 binding site, potentially regulating eRF1 binding to eRF3 in a competitive manner.
Crystal structure and functional analysis of the eukaryotic class II release factor eRF3 from S. pombe.,Kong C, Ito K, Walsh MA, Wada M, Liu Y, Kumar S, Barford D, Nakamura Y, Song H Mol Cell. 2004 Apr 23;14(2):233-45. PMID:15099522[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kong C, Ito K, Walsh MA, Wada M, Liu Y, Kumar S, Barford D, Nakamura Y, Song H. Crystal structure and functional analysis of the eukaryotic class II release factor eRF3 from S. pombe. Mol Cell. 2004 Apr 23;14(2):233-45. PMID:15099522
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