3v60: Difference between revisions
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<StructureSection load='3v60' size='340' side='right'caption='[[3v60]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='3v60' size='340' side='right'caption='[[3v60]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3v60]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3v60]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V60 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V60 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]] 2.6Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id=' | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3v60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v60 OCA], [https://pdbe.org/3v60 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v60 RCSB], [https://www.ebi.ac.uk/pdbsum/3v60 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v60 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=3v60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v60 OCA], [https://pdbe.org/3v60 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v60 RCSB], [https://www.ebi.ac.uk/pdbsum/3v60 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v60 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/SMT3_YEAST SMT3_YEAST] Not known; suppressor of MIF2 mutations. | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Saccharomyces cerevisiae S288C]] | ||
[[Category: | [[Category: Armstrong AA]] | ||
[[Category: | [[Category: Lima CD]] | ||
[[Category: | [[Category: Mohideen F]] | ||
Latest revision as of 13:33, 6 November 2024
Structure of S. cerevisiae PCNA conjugated to SUMO on lysine 164Structure of S. cerevisiae PCNA conjugated to SUMO on lysine 164
Structural highlights
FunctionSMT3_YEAST Not known; suppressor of MIF2 mutations. Publication Abstract from PubMedUbiquitin (Ub) and ubiquitin-like (Ubl) modifiers such as SUMO (also known as Smt3 in Saccharomyces cerevisiae) mediate signal transduction through post-translational modification of substrate proteins in pathways that control differentiation, apoptosis and the cell cycle, and responses to stress such as the DNA damage response. In yeast, the proliferating cell nuclear antigen PCNA (also known as Pol30) is modified by ubiquitin in response to DNA damage and by SUMO during S phase. Whereas Ub-PCNA can signal for recruitment of translesion DNA polymerases, SUMO-PCNA signals for recruitment of the anti-recombinogenic DNA helicase Srs2. It remains unclear how receptors such as Srs2 specifically recognize substrates after conjugation to Ub and Ubls. Here we show, through structural, biochemical and functional studies, that the Srs2 carboxy-terminal domain harbours tandem receptor motifs that interact independently with PCNA and SUMO and that both motifs are required to recognize SUMO-PCNA specifically. The mechanism presented is pertinent to understanding how other receptors specifically recognize Ub- and Ubl-modified substrates to facilitate signal transduction. Recognition of SUMO-modified PCNA requires tandem receptor motifs in Srs2.,Armstrong AA, Mohideen F, Lima CD Nature. 2012 Feb 29;483(7387):59-63. doi: 10.1038/nature10883. PMID:22382979[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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