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| | ==Crystal Structure of S. Cerevisiae SUMO E3 Ligase SIZ1== | | ==Crystal Structure of S. Cerevisiae SUMO E3 Ligase SIZ1== |
| - | <StructureSection load='3i2d' size='340' side='right' caption='[[3i2d]], [[Resolution|resolution]] 2.60Å' scene=''> | + | <StructureSection load='3i2d' size='340' side='right'caption='[[3i2d]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3i2d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3I2D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3I2D FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3i2d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3I2D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3I2D FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SIZ1, ULL1, YDR409W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SIZ1, ULL1, YDR409W ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=3i2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i2d OCA], [http://pdbe.org/3i2d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3i2d RCSB], [http://www.ebi.ac.uk/pdbsum/3i2d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3i2d 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=3i2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i2d OCA], [https://pdbe.org/3i2d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3i2d RCSB], [https://www.ebi.ac.uk/pdbsum/3i2d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3i2d ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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> | + | [[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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Atcc 18824]] | | [[Category: Atcc 18824]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Lima, C D]] | | [[Category: Lima, C D]] |
| | [[Category: Yunus, A A]] | | [[Category: Yunus, A A]] |
| Structural highlights
Function
[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]
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
Siz1 is a founding member of the Siz/PIAS RING family of SUMO E3 ligases. The X-ray structure of an active Siz1 ligase revealed an elongated tripartite architecture comprised of an N-terminal PINIT domain, a central zinc-containing RING-like SP-RING domain, and a C-terminal domain we term the SP-CTD. Structure-based mutational analysis and biochemical studies show that the SP-RING and SP-CTD are required for activation of the E2 approximately SUMO thioester, while the PINIT domain is essential for redirecting SUMO conjugation to the proliferating cell nuclear antigen (PCNA) at lysine 164, a nonconsensus lysine residue that is not modified by the SUMO E2 in the absence of Siz1. Mutational analysis of Siz1 and PCNA revealed surfaces on both proteins that are required for efficient SUMO modification of PCNA in vitro and in vivo.
Structure of the Siz/PIAS SUMO E3 ligase Siz1 and determinants required for SUMO modification of PCNA.,Yunus AA, Lima CD Mol Cell. 2009 Sep 11;35(5):669-82. PMID:19748360[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
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
- ↑ Yunus AA, Lima CD. Structure of the Siz/PIAS SUMO E3 ligase Siz1 and determinants required for SUMO modification of PCNA. Mol Cell. 2009 Sep 11;35(5):669-82. PMID:19748360 doi:S1097-2765(09)00508-5
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