3e20: Difference between revisions
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<StructureSection load='3e20' size='340' side='right'caption='[[3e20]], [[Resolution|resolution]] 3.50Å' scene=''> | <StructureSection load='3e20' size='340' side='right'caption='[[3e20]], [[Resolution|resolution]] 3.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3e20]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3e20]] is a 8 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=3E20 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E20 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5Å</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=3e20 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e20 OCA], [https://pdbe.org/3e20 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e20 RCSB], [https://www.ebi.ac.uk/pdbsum/3e20 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e20 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=3e20 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e20 OCA], [https://pdbe.org/3e20 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e20 RCSB], [https://www.ebi.ac.uk/pdbsum/3e20 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e20 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[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: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Cheng | [[Category: Schizosaccharomyces pombe]] | ||
[[Category: Kong | [[Category: Cheng Z]] | ||
[[Category: Lim | [[Category: Kong C]] | ||
[[Category: Song | [[Category: Lim M]] | ||
[[Category: Song H]] | |||
Latest revision as of 18:16, 1 November 2023
Crystal structure of S.pombe eRF1/eRF3 complexCrystal structure of S.pombe eRF1/eRF3 complex
Structural highlights
FunctionERF3_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 PubMedEukaryotic 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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