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3wxg

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'''Unreleased structure'''
 
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The entry 3wxg is ON HOLD until Paper Publication
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==Crystal structure of CYLD USP domain (C596A) in complex with Lys63-linked diubiquitin==
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<StructureSection load='3wxg' size='340' side='right'caption='[[3wxg]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3wxg]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio] 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=3WXG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WXG 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]] 3.1&#8491;</td></tr>
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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=3wxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wxg OCA], [https://pdbe.org/3wxg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wxg RCSB], [https://www.ebi.ac.uk/pdbsum/3wxg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wxg ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/E7FEV5_DANRE E7FEV5_DANRE]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The tumor suppressor CYLD belongs to a ubiquitin (Ub)-specific protease (USP) family and specifically cleaves Met1- and Lys63-linked polyubiquitin chains to suppress inflammatory signaling pathways. Here, we report crystal structures representing the catalytic states of zebrafish CYLD for Met1- and Lys63-linked Ub chains and two distinct precatalytic states for Met1-linked chains. In both catalytic states, the distal Ub is bound to CYLD in a similar manner, and the scissile bond is located close to the catalytic residue, whereas the proximal Ub is bound in a manner specific to Met1- or Lys63-linked chains. Further structure-based mutagenesis experiments support the mechanism by which CYLD specifically cleaves both Met1- and Lys63-linked chains and provide insight into tumor-associated mutations of CYLD. This study provides new structural insight into the mechanisms by which USP family deubiquitinating enzymes recognize and cleave Ub chains with specific linkage types.
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Authors: Sato, Y., Fukai, S.
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Structures of CYLD USP with Met1- or Lys63-linked diubiquitin reveal mechanisms for dual specificity.,Sato Y, Goto E, Shibata Y, Kubota Y, Yamagata A, Goto-Ito S, Kubota K, Inoue J, Takekawa M, Tokunaga F, Fukai S Nat Struct Mol Biol. 2015 Mar;22(3):222-9. doi: 10.1038/nsmb.2970. Epub 2015 Feb , 16. PMID:25686088<ref>PMID:25686088</ref>
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Description: Crystal structure of the ubiquitin protease in the K63-catalyltic state
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Sato, Y]]
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<div class="pdbe-citations 3wxg" style="background-color:#fffaf0;"></div>
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[[Category: Fukai, S]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Danio rerio]]
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[[Category: Large Structures]]
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[[Category: Mus musculus]]
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[[Category: Fukai S]]
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[[Category: Sato Y]]

Current revision

Crystal structure of CYLD USP domain (C596A) in complex with Lys63-linked diubiquitin

PDB ID 3wxg

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