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| | <StructureSection load='2ckh' size='340' side='right'caption='[[2ckh]], [[Resolution|resolution]] 3.20Å' scene=''> | | <StructureSection load='2ckh' size='340' side='right'caption='[[2ckh]], [[Resolution|resolution]] 3.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ckh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2bzo 2bzo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CKH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CKH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ckh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2bzo 2bzo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CKH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CKH FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1wm2|1wm2]], [[1wm3|1wm3]], [[1wz0|1wz0]], [[2ckg|2ckg]]</div></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]] 3.2Å</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=2ckh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ckh OCA], [https://pdbe.org/2ckh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ckh RCSB], [https://www.ebi.ac.uk/pdbsum/2ckh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ckh 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=2ckh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ckh OCA], [https://pdbe.org/2ckh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ckh RCSB], [https://www.ebi.ac.uk/pdbsum/2ckh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ckh ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/SENP1_HUMAN SENP1_HUMAN]] Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SUMO1, SUMO2 and SUMO3 to their mature forms and deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins. Deconjugates SUMO1 from HIPK2. Deconjugates SUMO1 from HDAC1, which decreases its transcriptional repression activity.<ref>PMID:10652325</ref> <ref>PMID:15199155</ref> <ref>PMID:16253240</ref> <ref>PMID:16553580</ref> [[https://www.uniprot.org/uniprot/SUMO2_HUMAN SUMO2_HUMAN]] Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Polymeric SUMO2 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins.<ref>PMID:9556629</ref> <ref>PMID:18538659</ref> <ref>PMID:18408734</ref>
| + | [https://www.uniprot.org/uniprot/SENP1_HUMAN SENP1_HUMAN] Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SUMO1, SUMO2 and SUMO3 to their mature forms and deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins. Deconjugates SUMO1 from HIPK2. Deconjugates SUMO1 from HDAC1, which decreases its transcriptional repression activity.<ref>PMID:10652325</ref> <ref>PMID:15199155</ref> <ref>PMID:16253240</ref> <ref>PMID:16553580</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: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dong, C]] | + | [[Category: Dong C]] |
| - | [[Category: Hay, R T]] | + | [[Category: Hay RT]] |
| - | [[Category: Liu, H]] | + | [[Category: Liu H]] |
| - | [[Category: Naismith, J H]] | + | [[Category: Naismith JH]] |
| - | [[Category: Shen, L N]] | + | [[Category: Shen LN]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Nuclear protein]]
| + | |
| - | [[Category: Protease]]
| + | |
| - | [[Category: Protease co- complex]]
| + | |
| - | [[Category: Sumo]]
| + | |
| - | [[Category: Thiol protease]]
| + | |
| - | [[Category: Ubl conjugation pathway]]
| + | |
| Structural highlights
Function
SENP1_HUMAN Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SUMO1, SUMO2 and SUMO3 to their mature forms and deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins. Deconjugates SUMO1 from HIPK2. Deconjugates SUMO1 from HDAC1, which decreases its transcriptional repression activity.[1] [2] [3] [4]
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
The SUMO (small ubiquitin-like modifier)-specific protease SENP1 (sentrin-specific protease 1) can process the three forms of SUMO to their mature forms and deconjugate SUMO from modified substrates. It has been demonstrated previously that SENP1 processed SUMO-1 more efficiently than SUMO-2, but displayed little difference in its ability to deconjugate the different SUMO paralogues from modified substrates. To determine the basis for this substrate specificity, we have determined the crystal structure of SENP1 in isolation and in a transition-state complex with SUMO-2. The interface between SUMO-2 and SENP1 has a relatively poor complementarity, and most of the recognition is determined by interaction between the conserved C-terminus of SUMO-2 and the cleft in the protease. Although SENP1 is rather similar in structure to the related protease SENP2, these proteases have different SUMO-processing activities. Electrostatic analysis of SENP1 in the region where the C-terminal peptide, removed during maturation, would project indicates that it is the electrostatic complementarity between this region of SENP1 and the C-terminal peptides of the various SUMO paralogues that mediates selectivity.
The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing.,Shen LN, Dong C, Liu H, Naismith JH, Hay RT Biochem J. 2006 Jul 15;397(2):279-88. PMID:16553580[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gong L, Millas S, Maul GG, Yeh ET. Differential regulation of sentrinized proteins by a novel sentrin-specific protease. J Biol Chem. 2000 Feb 4;275(5):3355-9. PMID:10652325
- ↑ Cheng J, Wang D, Wang Z, Yeh ET. SENP1 enhances androgen receptor-dependent transcription through desumoylation of histone deacetylase 1. Mol Cell Biol. 2004 Jul;24(13):6021-8. PMID:15199155 doi:10.1128/MCB.24.13.6021-6028.2004
- ↑ Kim YH, Sung KS, Lee SJ, Kim YO, Choi CY, Kim Y. Desumoylation of homeodomain-interacting protein kinase 2 (HIPK2) through the cytoplasmic-nuclear shuttling of the SUMO-specific protease SENP1. FEBS Lett. 2005 Nov 7;579(27):6272-8. Epub 2005 Oct 19. PMID:16253240 doi:S0014-5793(05)01251-2
- ↑ Shen LN, Dong C, Liu H, Naismith JH, Hay RT. The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing. Biochem J. 2006 Jul 15;397(2):279-88. PMID:16553580 doi:10.1042/BJ20052030
- ↑ Shen LN, Dong C, Liu H, Naismith JH, Hay RT. The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing. Biochem J. 2006 Jul 15;397(2):279-88. PMID:16553580 doi:10.1042/BJ20052030
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