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3tmo
From Proteopedia
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| - | [[Image:3tmo.png|left|200px]] | ||
| - | < | + | ==The catalytic domain of human deubiquitinase DUBA== |
| - | + | <StructureSection load='3tmo' size='340' side='right'caption='[[3tmo]], [[Resolution|resolution]] 2.20Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | or the | + | <table><tr><td colspan='2'>[[3tmo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TMO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TMO FirstGlance]. <br> |
| - | + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |
| - | - | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3tmp|3tmp]]</div></td></tr> |
| - | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DUBA, OTUD5 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | |
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ubiquitinyl_hydrolase_1 Ubiquitinyl hydrolase 1], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.12 3.4.19.12] </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=3tmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tmo OCA], [https://pdbe.org/3tmo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tmo RCSB], [https://www.ebi.ac.uk/pdbsum/3tmo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tmo ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/OTUD5_HUMAN OTUD5_HUMAN]] Deubiquitinating enzyme that functions as negative regulator of the innate immune system. Acts via TRAF3 deubiquitination and subsequent suppression of type I interferon (IFN) production. Has peptidase activity towards 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. Can also cleave 'Lys-11'-linked ubiquitin chains (in vitro).<ref>PMID:17991829</ref> <ref>PMID:22245969</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Addition and removal of ubiquitin or ubiquitin chains to and from proteins is a tightly regulated process that contributes to cellular signaling and protein stability. Here we show that phosphorylation of the human deubiquitinase DUBA (OTUD5) at a single residue, Ser177, is both necessary and sufficient to activate the enzyme. The crystal structure of the ubiquitin aldehyde adduct of active DUBA reveals a marked cooperation between phosphorylation and substrate binding. An intricate web of interactions involving the phosphate and the C-terminal tail of ubiquitin cause DUBA to fold around its substrate, revealing why phosphorylation is essential for deubiquitinase activity. Phosphoactivation of DUBA represents an unprecedented mode of protease regulation and a clear link between two major cellular signal transduction systems: phosphorylation and ubiquitin modification. | ||
| - | + | Phosphorylation-dependent activity of the deubiquitinase DUBA.,Huang OW, Ma X, Yin J, Flinders J, Maurer T, Kayagaki N, Phung Q, Bosanac I, Arnott D, Dixit VM, Hymowitz SG, Starovasnik MA, Cochran AG Nat Struct Mol Biol. 2012 Jan 15;19(2):171-5. doi: 10.1038/nsmb.2206. PMID:22245969<ref>PMID:22245969</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3tmo" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | == | + | [[Category: Human]] |
| - | + | [[Category: Large Structures]] | |
| - | + | ||
| - | == | + | |
| - | < | + | |
| - | [[Category: | + | |
[[Category: Ubiquitinyl hydrolase 1]] | [[Category: Ubiquitinyl hydrolase 1]] | ||
| - | [[Category: Bosanac, I | + | [[Category: Bosanac, I]] |
| - | [[Category: Cochran, A | + | [[Category: Cochran, A]] |
| - | [[Category: Hymowitz, S | + | [[Category: Hymowitz, S]] |
| - | [[Category: Ma, X | + | [[Category: Ma, X]] |
| - | [[Category: Starovasnik, M | + | [[Category: Starovasnik, M]] |
| - | [[Category: Yin, J | + | [[Category: Yin, J]] |
[[Category: Deubiquitinase]] | [[Category: Deubiquitinase]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Otu fold]] | [[Category: Otu fold]] | ||
[[Category: Phosphorylation]] | [[Category: Phosphorylation]] | ||
Current revision
The catalytic domain of human deubiquitinase DUBA
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