3tmp

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[[Image:3tmp.png|left|200px]]
 
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==The catalytic domain of human deubiquitinase DUBA in complex with ubiquitin aldehyde==
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The line below this paragraph, containing "STRUCTURE_3tmp", creates the "Structure Box" on the page.
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<StructureSection load='3tmp' size='340' side='right'caption='[[3tmp]], [[Resolution|resolution]] 1.91&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3tmp]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TMP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TMP FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.91&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLZ:AMINO-ACETALDEHYDE'>GLZ</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
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{{STRUCTURE_3tmp| PDB=3tmp | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3tmp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tmp OCA], [https://pdbe.org/3tmp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tmp RCSB], [https://www.ebi.ac.uk/pdbsum/3tmp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tmp ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===The catalytic domain of human deubiquitinase DUBA in complex with ubiquitin aldehyde===
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3tmp" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_22245969}}, adds the Publication Abstract to the page
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*[[3D structures of ubiquitin|3D structures of ubiquitin]]
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(as it appears on PubMed at http://www.pubmed.gov), where 22245969 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_22245969}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[3tmp]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TMP OCA].
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==Reference==
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<ref group="xtra">PMID:022245969</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Ubiquitinyl hydrolase 1]]
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[[Category: Large Structures]]
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[[Category: Cochran, A.]]
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[[Category: Cochran A]]
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[[Category: Hymowitz, S.]]
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[[Category: Hymowitz S]]
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[[Category: Ma, X.]]
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[[Category: Ma X]]
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[[Category: Starovasnik, M.]]
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[[Category: Starovasnik M]]
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[[Category: Yin, J.]]
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[[Category: Yin J]]
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[[Category: Deubiquitinase]]
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[[Category: Hydrolase-protein binding complex]]
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[[Category: Otu fold]]
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[[Category: Phosphorylation]]
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Current revision

The catalytic domain of human deubiquitinase DUBA in complex with ubiquitin aldehyde

PDB ID 3tmp

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