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| | <StructureSection load='5jne' size='340' side='right'caption='[[5jne]], [[Resolution|resolution]] 2.85Å' scene=''> | | <StructureSection load='5jne' size='340' side='right'caption='[[5jne]], [[Resolution|resolution]] 2.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5jne]] is a 8 chain structure with sequence from [http://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=5JNE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JNE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5jne]] is a 8 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=5JNE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JNE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6LN:ETHANE-1,2-DITHIOL'>6LN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.85Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SMT3, YDR510W, D9719.15 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), UBC9, YDL064W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), POL30, YBR088C, YBR0811 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6LN:ETHANE-1,2-DITHIOL'>6LN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5jne FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jne OCA], [http://pdbe.org/5jne PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jne RCSB], [http://www.ebi.ac.uk/pdbsum/5jne PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jne 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=5jne FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jne OCA], [https://pdbe.org/5jne PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jne RCSB], [https://www.ebi.ac.uk/pdbsum/5jne PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jne ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> [[http://www.uniprot.org/uniprot/SIZ1_YEAST SIZ1_YEAST]] Acts as an E3 ligase mediating SUMO/Smt3 attachment to septins and PCNA. May be involved in chromosome maintenance.<ref>PMID:11572779</ref> <ref>PMID:11587849</ref> <ref>PMID:11333221</ref> <ref>PMID:11577116</ref> <ref>PMID:12226657</ref> [[http://www.uniprot.org/uniprot/SMT3_YEAST SMT3_YEAST]] Not known; suppressor of MIF2 mutations. [[http://www.uniprot.org/uniprot/UBC9_YEAST UBC9_YEAST]] E2 ubiquitin-like--protein ligase mediating SUMO/Smt3 attachment to septins and PCNA. Seems to be involved in degradation of S- (CLB5) and M-phase cyclins (CLB2).<ref>PMID:9341106</ref> <ref>PMID:11572779</ref> | + | [https://www.uniprot.org/uniprot/SMT3_YEAST SMT3_YEAST] Not known; suppressor of MIF2 mutations.[https://www.uniprot.org/uniprot/SIZ1_YEAST SIZ1_YEAST] Acts as an E3 ligase mediating SUMO/Smt3 attachment to septins and PCNA. May be involved in chromosome maintenance.<ref>PMID:11572779</ref> <ref>PMID:11587849</ref> <ref>PMID:11333221</ref> <ref>PMID:11577116</ref> <ref>PMID:12226657</ref> |
| | <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: Baker's yeast]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lima, C D]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Streich, F C]] | + | [[Category: Lima CD]] |
| - | [[Category: E2 conjugating enzyme]] | + | [[Category: Streich Jr FC]] |
| - | [[Category: E3 ligase]]
| + | |
| - | [[Category: Ligase-signaling protein complex]]
| + | |
| - | [[Category: Pia]]
| + | |
| - | [[Category: Siz]]
| + | |
| - | [[Category: Substrate complex]]
| + | |
| - | [[Category: Sumo]]
| + | |
| - | [[Category: Ubiquitin]]
| + | |
| - | [[Category: Ubiquitin-like]]
| + | |
| Structural highlights
Function
SMT3_YEAST Not known; suppressor of MIF2 mutations.SIZ1_YEAST Acts as an E3 ligase mediating SUMO/Smt3 attachment to septins and PCNA. May be involved in chromosome maintenance.[1] [2] [3] [4] [5]
Publication Abstract from PubMed
Post-translational protein modification by ubiquitin (Ub) and ubiquitin-like (Ubl) proteins such as small ubiquitin-like modifier (SUMO) regulates processes including protein homeostasis, the DNA damage response, and the cell cycle. Proliferating cell nuclear antigen (PCNA) is modified by Ub or poly-Ub at lysine (Lys)164 after DNA damage to recruit repair factors. Yeast PCNA is modified by SUMO on Lys164 and Lys127 during S-phase to recruit the anti-recombinogenic helicase Srs2. Lys164 modification requires specialized E2/E3 enzyme pairs for SUMO or Ub conjugation. For SUMO, Lys164 modification is strictly dependent on the E3 ligase Siz1, suggesting the E3 alters E2 specificity to promote Lys164 modification. The structural basis for substrate interactions in activated E3/E2-Ub/Ubl complexes remains unclear. Here we report an engineered E2 protein and cross-linking strategies that trap an E3/E2-Ubl/substrate complex for structure determination, illustrating how an E3 can bypass E2 specificity to force-feed a substrate lysine into the E2 active site.
Capturing a substrate in an activated RING E3/E2-SUMO complex.,Streich FC Jr, Lima CD Nature. 2016 Aug 18;536(7616):304-8. PMID:27509863[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Johnson ES, Gupta AA. An E3-like factor that promotes SUMO conjugation to the yeast septins. Cell. 2001 Sep 21;106(6):735-44. PMID:11572779
- ↑ Takahashi Y, Toh-e A, Kikuchi Y. A novel factor required for the SUMO1/Smt3 conjugation of yeast septins. Gene. 2001 Sep 19;275(2):223-31. PMID:11587849
- ↑ Strunnikov AV, Aravind L, Koonin EV. Saccharomyces cerevisiae SMT4 encodes an evolutionarily conserved protease with a role in chromosome condensation regulation. Genetics. 2001 May;158(1):95-107. PMID:11333221
- ↑ Takahashi Y, Kahyo T, Toh-E A, Yasuda H, Kikuchi Y. Yeast Ull1/Siz1 is a novel SUMO1/Smt3 ligase for septin components and functions as an adaptor between conjugating enzyme and substrates. J Biol Chem. 2001 Dec 28;276(52):48973-7. Epub 2001 Sep 27. PMID:11577116 doi:http://dx.doi.org/10.1074/jbc.M109295200
- ↑ Hoege C, Pfander B, Moldovan GL, Pyrowolakis G, Jentsch S. RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature. 2002 Sep 12;419(6903):135-41. PMID:12226657 doi:10.1038/nature00991
- ↑ Streich FC Jr, Lima CD. Capturing a substrate in an activated RING E3/E2-SUMO complex. Nature. 2016 Aug 18;536(7616):304-8. PMID:27509863 doi:http://dx.doi.org/10.1038/nature19071
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