3tmo

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[[Image:3tmo.png|left|200px]]
 
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==The catalytic domain of human deubiquitinase DUBA==
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The line below this paragraph, containing "STRUCTURE_3tmo", creates the "Structure Box" on the page.
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<StructureSection load='3tmo' size='340' side='right'caption='[[3tmo]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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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'>[[3tmo]] is a 1 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=3TMO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TMO 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]] 2.2&#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=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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{{STRUCTURE_3tmo| PDB=3tmo | 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=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>
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</table>
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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===
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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 3tmo" style="background-color:#fffaf0;"></div>
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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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[[3tmo]] is a 1 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=3TMO 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: Bosanac, I.]]
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[[Category: Bosanac I]]
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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]]
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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

PDB ID 3tmo

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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