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5fq2
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of human SUMO E1 UFD domain in complex with Ubc9 in a P422 space group.== | |
| + | <StructureSection load='5fq2' size='340' side='right' caption='[[5fq2]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5fq2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FQ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FQ2 FirstGlance]. <br> | ||
| + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LDH:N~6~-ETHYL-L-LYSINE'>LDH</scene>, <scene name='pdbligand=MLZ:N-METHYL-LYSINE'>MLZ</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=5fq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fq2 OCA], [http://pdbe.org/5fq2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fq2 RCSB], [http://www.ebi.ac.uk/pdbsum/5fq2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fq2 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/UBC9_HUMAN UBC9_HUMAN]] Accepts the ubiquitin-like proteins SUMO1, SUMO2, SUMO3 and SUMO4 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. Necessary for sumoylation of FOXL2 and KAT5. Essential for nuclear architecture and chromosome segregation.<ref>PMID:8668529</ref> <ref>PMID:11451954</ref> <ref>PMID:15809060</ref> <ref>PMID:19744555</ref> <ref>PMID:19638400</ref> <ref>PMID:17466333</ref> <ref>PMID:20077568</ref> [[http://www.uniprot.org/uniprot/SAE2_HUMAN SAE2_HUMAN]] The heterodimer acts as a E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. It mediates ATP-dependent activation of SUMO proteins followed by formation of a thioester bond between a SUMO protein and a conserved active site cysteine residue on UBA2/SAE2.<ref>PMID:11481243</ref> <ref>PMID:11451954</ref> <ref>PMID:19443651</ref> <ref>PMID:15660128</ref> <ref>PMID:17643372</ref> <ref>PMID:20164921</ref> | ||
| - | + | ==See Also== | |
| - | + | *[[Ubiquitin activating enzyme|Ubiquitin activating enzyme]] | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Castano, L]] | ||
| + | [[Category: Liu, B]] | ||
| + | [[Category: Lois, M]] | ||
[[Category: Reverter, D]] | [[Category: Reverter, D]] | ||
| - | [[Category: | + | [[Category: Activating enzyme]] |
| - | [[Category: | + | [[Category: Conjugating enzyme]] |
| - | [[Category: | + | [[Category: Ligase]] |
| + | [[Category: Sumo]] | ||
Revision as of 03:24, 10 December 2016
Crystal structure of human SUMO E1 UFD domain in complex with Ubc9 in a P422 space group.
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Categories: Castano, L | Liu, B | Lois, M | Reverter, D | Activating enzyme | Conjugating enzyme | Ligase | Sumo
