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| | <StructureSection load='2hl8' size='340' side='right'caption='[[2hl8]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='2hl8' size='340' side='right'caption='[[2hl8]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2hl8]] 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=2HL8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HL8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2hl8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HL8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HL8 FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</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]] 2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2hkp|2hkp]], [[2hl9|2hl9]], [[1euv|1euv]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene></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=2hl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hl8 OCA], [https://pdbe.org/2hl8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hl8 RCSB], [https://www.ebi.ac.uk/pdbsum/2hl8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hl8 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=2hl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hl8 OCA], [https://pdbe.org/2hl8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hl8 RCSB], [https://www.ebi.ac.uk/pdbsum/2hl8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hl8 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/ULP1_YEAST ULP1_YEAST]] Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SMT3 to its mature form and deconjugation of SMT3 from targeted proteins. Has an essential role in the G2/M phase of the cell cycle.<ref>PMID:10094048</ref>
| + | [https://www.uniprot.org/uniprot/ULP1_YEAST ULP1_YEAST] Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SMT3 to its mature form and deconjugation of SMT3 from targeted proteins. Has an essential role in the G2/M phase of the cell cycle.<ref>PMID:10094048</ref> |
| | == 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: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Au, S W.N]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Ng, T B]] | + | [[Category: Au SWN]] |
| - | [[Category: Xu, Z]] | + | [[Category: Ng TB]] |
| - | [[Category: Hydrolase]] | + | [[Category: Xu Z]] |
| Structural highlights
Function
ULP1_YEAST Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SMT3 to its mature form and deconjugation of SMT3 from targeted proteins. Has an essential role in the G2/M phase of the cell cycle.[1]
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
Sumoylation has emerged as an indispensable post-translational modification that modulates the functions of a broad spectrum of proteins. Recent studies have demonstrated that reactive oxygen species influence the equilibrium of sumoylation-desumoylation. We show herein that H2O2 induces formation of an intermolecular disulfide linkage of human SUMO protease SENP1 via the active-site Cys 603 and a unique residue Cys 613. Such reversible modification confers a higher recovery of enzyme activity, which is also observed in yeast Ulp1, but not in human SENP2, suggesting its protective role against irreversible sulfhydryl oxidation. In vivo formation of a disulfide-linked dimer of SENP1 is also detected in cultured cells in response to oxidative stress. The modifications are further elucidated by the crystal structures of Ulp1 with the catalytic cysteine oxidized to sulfenic, sulfinic, and sulfonic acids. Our findings suggest that, in addition to SUMO conjugating enzymes, SUMO proteases may act as redox sensors and effectors modulating the desumoylation pathway and specific cellular responses to oxidative stress.
Molecular basis of the redox regulation of SUMO proteases: a protective mechanism of intermolecular disulfide linkage against irreversible sulfhydryl oxidation.,Xu Z, Lam LS, Lam LH, Chau SF, Ng TB, Au SW FASEB J. 2008 Jan;22(1):127-37. Epub 2007 Aug 17. PMID:17704192[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Li SJ, Hochstrasser M. A new protease required for cell-cycle progression in yeast. Nature. 1999 Mar 18;398(6724):246-51. PMID:10094048 doi:http://dx.doi.org/10.1038/18457
- ↑ Xu Z, Lam LS, Lam LH, Chau SF, Ng TB, Au SW. Molecular basis of the redox regulation of SUMO proteases: a protective mechanism of intermolecular disulfide linkage against irreversible sulfhydryl oxidation. FASEB J. 2008 Jan;22(1):127-37. Epub 2007 Aug 17. PMID:17704192 doi:10.1096/fj.06-7871com
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