3oj3

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[[Image:3oj3.png|left|200px]]
 
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{{STRUCTURE_3oj3| PDB=3oj3 | SCENE= }}
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==Crystal structure of the A20 ZnF4 and ubiquitin complex==
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<StructureSection load='3oj3' size='340' side='right'caption='[[3oj3]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3oj3]] is a 16 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=3OJ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OJ3 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]] 2.5&#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=ZN:ZINC+ION'>ZN</scene></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=3oj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oj3 OCA], [https://pdbe.org/3oj3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oj3 RCSB], [https://www.ebi.ac.uk/pdbsum/3oj3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oj3 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/UBB_HUMAN UBB_HUMAN] 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:16543144</ref> <ref>PMID:19754430</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Inactivating mutations in the ubiquitin (Ub) editing protein A20 promote persistent nuclear factor (NF)-kappaB signaling and are genetically linked to inflammatory diseases and hematologic cancers. A20 tightly regulates NF-kappaB signaling by acting as an Ub editor, removing K63-linked Ub chains and mediating addition of Ub chains that target substrates for degradation. However, a precise molecular understanding of how A20 modulates this pathway remains elusive. Here, using structural analysis, domain mapping, and functional assays, we show that A20 zinc finger 4 (ZnF4) does not directly interact with E2 enzymes but instead can bind mono-Ub and K63-linked poly-Ub. Mutations to the A20 ZnF4 Ub-binding surface result in decreased A20-mediated ubiquitination and impaired regulation of NF-kappaB signaling. Collectively, our studies illuminate the mechanistically distinct but biologically interdependent activities of the A20 ZnF and ovarian tumor (OTU) domains that are inherent to the Ub editing process and, ultimately, to regulation of NF-kappaB signaling.
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===Crystal structure of the A20 ZnF4 and ubiquitin complex===
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Ubiquitin Binding to A20 ZnF4 Is Required for Modulation of NF-kappaB Signaling.,Bosanac I, Wertz IE, Pan B, Yu C, Kusam S, Lam C, Phu L, Phung Q, Maurer B, Arnott D, Kirkpatrick DS, Dixit VM, Hymowitz SG Mol Cell. 2010 Nov 24;40(4):548-57. PMID:21095585<ref>PMID:21095585</ref>
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{{ABSTRACT_PUBMED_21095585}}
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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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==About this Structure==
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<div class="pdbe-citations 3oj3" style="background-color:#fffaf0;"></div>
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[[3oj3]] is a 16 chain structure of [[Ubiquitin]] 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=3OJ3 OCA].
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==See Also==
==See Also==
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*[[Ubiquitin|Ubiquitin]]
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*[[3D structures of ubiquitin|3D structures of ubiquitin]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:021095585</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Bosanac, I]]
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[[Category: Large Structures]]
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[[Category: Hymowitz, S G.]]
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[[Category: Bosanac I]]
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[[Category: Protein binding-hydrolase complex]]
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[[Category: Hymowitz SG]]
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[[Category: Ubiquitin]]
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[[Category: Zinc finger]]
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[[Category: Zinc ion]]
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Current revision

Crystal structure of the A20 ZnF4 and ubiquitin complex

PDB ID 3oj3

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