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| | <StructureSection load='2uyz' size='340' side='right'caption='[[2uyz]], [[Resolution|resolution]] 1.40Å' scene=''> | | <StructureSection load='2uyz' size='340' side='right'caption='[[2uyz]], [[Resolution|resolution]] 1.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2uyz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human] and [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UYZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2UYZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2uyz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UYZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2UYZ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1u9a|1u9a]], [[1u9b|1u9b]], [[1a5r|1a5r]], [[1tgz|1tgz]], [[1wyw|1wyw]], [[1y8r|1y8r]], [[1z5s|1z5s]], [[2asq|2asq]], [[2bf8|2bf8]], [[2g4d|2g4d]], [[2io2|2io2]], [[2iy0|2iy0]], [[2iy1|2iy1]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] </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=2uyz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uyz OCA], [https://pdbe.org/2uyz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2uyz RCSB], [https://www.ebi.ac.uk/pdbsum/2uyz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2uyz 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=2uyz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uyz OCA], [https://pdbe.org/2uyz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2uyz RCSB], [https://www.ebi.ac.uk/pdbsum/2uyz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2uyz ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/UBC9_MOUSE UBC9_MOUSE]] Accepts the ubiquitin-like proteins SUMO1, SUMO2 and SUMO3 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2 or CBX4. Can catalyze the formation of poly-SUMO chains. Essential for nuclear architecture, chromosome segregation and embryonic viability. Necessary for sumoylation of FOXL2 and KAT5 (By similarity).<ref>PMID:16326389</ref> <ref>PMID:17187077</ref>
| + | [https://www.uniprot.org/uniprot/UBC9_MOUSE UBC9_MOUSE] Accepts the ubiquitin-like proteins SUMO1, SUMO2 and SUMO3 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2 or CBX4. Can catalyze the formation of poly-SUMO chains. Essential for nuclear architecture, chromosome segregation and embryonic viability. Necessary for sumoylation of FOXL2 and KAT5 (By similarity).<ref>PMID:16326389</ref> <ref>PMID:17187077</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: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Ubiquitin--protein ligase]]
| + | [[Category: Knipscheer P]] |
| - | [[Category: Dijk, W J.van]]
| + | [[Category: Mann M]] |
| - | [[Category: Knipscheer, P]] | + | [[Category: Olsen JV]] |
| - | [[Category: Mann, M]] | + | [[Category: Sixma TK]] |
| - | [[Category: Olsen, J V]] | + | [[Category: Van Dijk WJ]] |
| - | [[Category: Sixma, T K]] | + | |
| - | [[Category: Cell cycle]] | + | |
| - | [[Category: Cell division]]
| + | |
| - | [[Category: Chromosome partition]]
| + | |
| - | [[Category: Conjugating enzyme]]
| + | |
| - | [[Category: E2]]
| + | |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: Mitosis]]
| + | |
| - | [[Category: Nuclear protein]]
| + | |
| - | [[Category: Sumo1]]
| + | |
| - | [[Category: Sumoylation]]
| + | |
| - | [[Category: Ubc9]]
| + | |
| - | [[Category: Ubiquitin-like modifier]]
| + | |
| - | [[Category: Ubl conjugation pathway]]
| + | |
| Structural highlights
Function
UBC9_MOUSE Accepts the ubiquitin-like proteins SUMO1, SUMO2 and SUMO3 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2 or CBX4. Can catalyze the formation of poly-SUMO chains. Essential for nuclear architecture, chromosome segregation and embryonic viability. Necessary for sumoylation of FOXL2 and KAT5 (By similarity).[1] [2]
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 ubiquitin-related modifier SUMO regulates a wide range of cellular processes by post-translational modification with one, or a chain of SUMO molecules. Sumoylation is achieved by the sequential action of several enzymes in which the E2, Ubc9, transfers SUMO from the E1 to the target mostly with the help of an E3 enzyme. In this process, Ubc9 not only forms a thioester bond with SUMO, but also interacts with SUMO noncovalently. Here, we show that this noncovalent interaction promotes the formation of short SUMO chains on targets such as Sp100 and HDAC4. We present a crystal structure of the noncovalent Ubc9-SUMO1 complex, showing that SUMO is located far from the E2 active site and resembles the noncovalent interaction site for ubiquitin on UbcH5c and Mms2. Structural comparison suggests a model for poly-sumoylation involving a mechanism analogous to Mms2-Ubc13-mediated ubiquitin chain formation.
Noncovalent interaction between Ubc9 and SUMO promotes SUMO chain formation.,Knipscheer P, van Dijk WJ, Olsen JV, Mann M, Sixma TK EMBO J. 2007 Jun 6;26(11):2797-807. Epub 2007 May 10. PMID:17491593[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nacerddine K, Lehembre F, Bhaumik M, Artus J, Cohen-Tannoudji M, Babinet C, Pandolfi PP, Dejean A. The SUMO pathway is essential for nuclear integrity and chromosome segregation in mice. Dev Cell. 2005 Dec;9(6):769-79. PMID:16326389 doi:S1534-5807(05)00389-8
- ↑ Park SW, Hu X, Gupta P, Lin YP, Ha SG, Wei LN. SUMOylation of Tr2 orphan receptor involves Pml and fine-tunes Oct4 expression in stem cells. Nat Struct Mol Biol. 2007 Jan;14(1):68-75. Epub 2006 Dec 24. PMID:17187077 doi:10.1038/nsmb1185
- ↑ Knipscheer P, van Dijk WJ, Olsen JV, Mann M, Sixma TK. Noncovalent interaction between Ubc9 and SUMO promotes SUMO chain formation. EMBO J. 2007 Jun 6;26(11):2797-807. Epub 2007 May 10. PMID:17491593
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