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3wxg

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==Crystal structure of CYLD USP domain (C596A) in complex with Lys63-linked diubiquitin==
==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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<StructureSection load='3wxg' size='340' side='right'caption='[[3wxg]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3wxg]] is a 6 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WXG FirstGlance]. <br>
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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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wxe|3wxe]], [[3wxf|3wxf]]</td></tr>
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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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wxg OCA], [http://pdbe.org/3wxg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wxg RCSB], [http://www.ebi.ac.uk/pdbsum/3wxg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wxg ProSAT]</span></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>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/UBC_MOUSE UBC_MOUSE]] Ubiquitin: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.<ref>PMID:19754430</ref>
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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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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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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 3wxg" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Fukai, S]]
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[[Category: Danio rerio]]
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[[Category: Sato, Y]]
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[[Category: Large Structures]]
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[[Category: Hydrolase-protein binding complex]]
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[[Category: Mus musculus]]
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[[Category: Ubiquitin protease]]
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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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