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| | ==Crystal structure of GFP-TAX1BP1 UBZ2 domain fusion protein== | | ==Crystal structure of GFP-TAX1BP1 UBZ2 domain fusion protein== |
| - | <StructureSection load='4z4m' size='340' side='right' caption='[[4z4m]], [[Resolution|resolution]] 2.15Å' scene=''> | + | <StructureSection load='4z4m' size='340' side='right'caption='[[4z4m]], [[Resolution|resolution]] 2.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4z4m]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aeqvi Aeqvi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z4M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Z4M FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4z4m]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z4M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Z4M FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CR2:{(4Z)-2-(AMINOMETHYL)-4-[(4-HYDROXYPHENYL)METHYLIDENE]-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>CR2</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CR2:{(4Z)-2-(AMINOMETHYL)-4-[(4-HYDROXYPHENYL)METHYLIDENE]-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>CR2</scene></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4z4m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z4m OCA], [https://pdbe.org/4z4m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4z4m RCSB], [https://www.ebi.ac.uk/pdbsum/4z4m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4z4m ProSAT]</span></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4z4k|4z4k]]</td></tr>
| + | |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TAX1BP1, T6BP, PRO0105 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6100 AEQVI])</td></tr>
| + | |
| - | <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=4z4m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z4m OCA], [http://pdbe.org/4z4m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4z4m RCSB], [http://www.ebi.ac.uk/pdbsum/4z4m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4z4m ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GFP_AEQVI GFP_AEQVI]] Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin. | + | [https://www.uniprot.org/uniprot/TAXB1_HUMAN TAXB1_HUMAN] Inhibits TNF-induced apoptosis by mediating the TNFAIP3 anti-apoptotic activity. Degraded by caspase-3-like family proteins upon TNF-induced apoptosis. May also play a role in the pro-inflammatory cytokine IL-1 signaling cascade.<ref>PMID:10435631</ref> <ref>PMID:10920205</ref> [https://www.uniprot.org/uniprot/GFP_AEQVI GFP_AEQVI] Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4z4m" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4z4m" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aeqvi]] | + | [[Category: Aequorea victoria]] |
| - | [[Category: Kawasaki, M]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Rohaim, A]] | + | [[Category: Large Structures]] |
| - | [[Category: Wakatsuki, S]] | + | [[Category: Kawasaki M]] |
| - | [[Category: Flurorescent protein]] | + | [[Category: Rohaim A]] |
| - | [[Category: Gfp]] | + | [[Category: Wakatsuki S]] |
| - | [[Category: Metal binding protein]]
| + | |
| - | [[Category: Tax1bp1]]
| + | |
| - | [[Category: Ubz]]
| + | |
| - | [[Category: Zinc-finger]]
| + | |
| Structural highlights
Function
TAXB1_HUMAN Inhibits TNF-induced apoptosis by mediating the TNFAIP3 anti-apoptotic activity. Degraded by caspase-3-like family proteins upon TNF-induced apoptosis. May also play a role in the pro-inflammatory cytokine IL-1 signaling cascade.[1] [2] GFP_AEQVI Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin.
Publication Abstract from PubMed
The ubiquitin-binding zinc finger (UBZ) is a type of zinc-coordinating beta-beta-alpha fold domain found mainly in proteins involved in DNA repair and transcriptional regulation. Here we report the crystal structure of the UBZ domain of Y-family DNA polymerase (pol) eta and the crystal structure of the complex between the UBZ domain of Werner helicase-interacting protein 1 (WRNIP1) and ubiquitin, crystallized using the green fluorescent protein fusion technique. In contrast to the pol eta UBZ, which has been proposed to bind ubiquitin via its C-terminal alpha helix, ubiquitin binds to a novel surface of WRNIP1 UBZ composed of the first beta strand and the C-terminal alpha helix. In addition, we report the structure of the tandem UBZ domains of Tax1-binding protein 1 (TAX1BP1) and show that the second UBZ of TAX1BP1 binds ubiquitin, presumably in a manner similar to that of WRNIP1 UBZ. We propose that UBZ domains can be divided into at least two different types in terms of the ubiquitin-binding surfaces: the pol eta type and the WRNIP1 type. This article is protected by copyright. All rights reserved.
A novel mode of ubiquitin recognition by the ubiquitin-binding zinc finger domain of WRNIP1.,Suzuki N, Rohaim A, Kato R, Dikic I, Wakatsuki S, Kawasaki M FEBS J. 2016 Apr 8. doi: 10.1111/febs.13734. PMID:27062441[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ De Valck D, Jin DY, Heyninck K, Van de Craen M, Contreras R, Fiers W, Jeang KT, Beyaert R. The zinc finger protein A20 interacts with a novel anti-apoptotic protein which is cleaved by specific caspases. Oncogene. 1999 Jul 22;18(29):4182-90. PMID:10435631 doi:http://dx.doi.org/10.1038/sj.onc.1202787
- ↑ Ling L, Goeddel DV. T6BP, a TRAF6-interacting protein involved in IL-1 signaling. Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9567-72. PMID:10920205 doi:http://dx.doi.org/10.1073/pnas.170279097
- ↑ Suzuki N, Rohaim A, Kato R, Dikic I, Wakatsuki S, Kawasaki M. A novel mode of ubiquitin recognition by the ubiquitin-binding zinc finger domain of WRNIP1. FEBS J. 2016 Apr 8. doi: 10.1111/febs.13734. PMID:27062441 doi:http://dx.doi.org/10.1111/febs.13734
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