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3v62

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Structure of the S. cerevisiae Srs2 C-terminal domain in complex with PCNA conjugated to SUMO on lysine 164

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Retrieved from "http://52.214.119.220/wiki/index.php/3v62"

Categories: Large Structures | Saccharomyces cerevisiae S288C | Armstrong AA | Lima CD | Mohideen F

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 <StructureSection load='3v62' size='340' side='right'caption='[[3v62]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3v62]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V62 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V62 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3v62]] is a 6 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=3V62 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V62 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NEQ:N-ETHYLMALEIMIDE'>NEQ</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.9&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene>, <scene name='pdbligand=NEQ:N-ETHYLMALEIMIDE'>NEQ</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3v60|3v60]], [[3v61|3v61]]</div></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">D9719.15, SMT3, YDR510W ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), POL30, YBR0811, YBR088C ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), HPR5, J0913, RADH, SRS2, YJL092W ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12] </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=3v62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v62 OCA], [https://pdbe.org/3v62 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v62 RCSB], [https://www.ebi.ac.uk/pdbsum/3v62 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v62 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/SMT3_YEAST SMT3_YEAST]] Not known; suppressor of MIF2 mutations. [[https://www.uniprot.org/uniprot/SRS2_YEAST SRS2_YEAST]] ATP-dependent DNA helicase involved in DNA repair at least for UV-induced lesions. The polarity of the helicase activity was determined to be 3' to 5'. [[https://www.uniprot.org/uniprot/PCNA_YEAST PCNA_YEAST]] This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. Involved in DNA repair.<ref>PMID:11545742</ref> <ref>PMID:12226657</ref>
+[https://www.uniprot.org/uniprot/SMT3_YEAST SMT3_YEAST] Not known; suppressor of MIF2 mutations.
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Ubiquitin (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<ref>PMID:22382979</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3v62" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Proliferating cell nuclear antigen 3D structures|Proliferating cell nuclear antigen 3D structures]]
 *[[SUMO 3D Structures|SUMO 3D Structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Baker's yeast]]
-[[Category: DNA helicase]]
 [[Category: Large Structures]]
-[[Category: Armstrong, A A]]
+[[Category: Saccharomyces cerevisiae S288C]]
-[[Category: Lima, C D]]
+[[Category: Armstrong AA]]
-[[Category: Mohideen, F]]
+[[Category: Lima CD]]
-[[Category: Nem modification on pcna cys22 and cys81 reductive methylation of all lysine residues on smt3]]
+[[Category: Mohideen F]]
-[[Category: Nuclear]]
-[[Category: Post-translational modification dna replication dna damage response]]
-[[Category: Protein binding-dna binding protein complex]]
-[[Category: Srs2]]
-[[Category: Ubiquitin-like protein pcna]]

3v62

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Structure of the S. cerevisiae Srs2 C-terminal domain in complex with PCNA conjugated to SUMO on lysine 164

Structural highlights

Function

See Also

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