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5vzv

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Current revision (14:13, 13 March 2024) (edit) (undo)
 
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<StructureSection load='5vzv' size='340' side='right'caption='[[5vzv]], [[Resolution|resolution]] 1.81&Aring;' scene=''>
<StructureSection load='5vzv' size='340' side='right'caption='[[5vzv]], [[Resolution|resolution]] 1.81&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5vzv]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VZV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VZV FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5vzv]] is a 3 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=5VZV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VZV FirstGlance]. <br>
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</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>
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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]] 1.812&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TRIM23, ARD1, ARFD1, RNF46 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RING-type_E3_ubiquitin_transferase RING-type E3 ubiquitin transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.27 2.3.2.27] </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=5vzv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vzv OCA], [https://pdbe.org/5vzv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vzv RCSB], [https://www.ebi.ac.uk/pdbsum/5vzv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vzv ProSAT]</span></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=5vzv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vzv OCA], [http://pdbe.org/5vzv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vzv RCSB], [http://www.ebi.ac.uk/pdbsum/5vzv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vzv ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/TRI23_HUMAN TRI23_HUMAN]] Acts as an E3 ubiquitin-protein ligase. In the presence of the human cytomegalovirus (HCMV) protein UL144, participates in 'Lys-63'-linked auto-ubiquitination of TRAF6 resulting in the virally controlled activation of NF-kappa-B at early time of infection. The C-terminus can act as an allosteric activator of the cholera toxin catalytic subunit.<ref>PMID:15684077</ref>
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[https://www.uniprot.org/uniprot/TRI23_HUMAN TRI23_HUMAN] Acts as an E3 ubiquitin-protein ligase. In the presence of the human cytomegalovirus (HCMV) protein UL144, participates in 'Lys-63'-linked auto-ubiquitination of TRAF6 resulting in the virally controlled activation of NF-kappa-B at early time of infection. The C-terminus can act as an allosteric activator of the cholera toxin catalytic subunit.<ref>PMID:15684077</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Tripartite motif (TRIM) proteins comprise a large family of RING-type ubiquitin E3 ligases that regulate important biological processes. An emerging general model is that TRIMs form elongated antiparallel coiled-coil dimers that prevent interaction of the two attendant RING domains. The RING domains themselves bind E2 conjugating enzymes as dimers, implying that an active TRIM ligase requires higher-order oligomerization of the basal coiled-coil dimers. Here, we report crystal structures of the TRIM23 RING domain in isolation and in complex with an E2-ubiquitin conjugate. Our results indicate that TRIM23 enzymatic activity requires RING dimerization, consistent with the general model of TRIM activation.
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Structure and catalytic activation of the TRIM23 RING E3 ubiquitin ligase.,Dawidziak DM, Sanchez JG, Wagner JM, Ganser-Pornillos BK, Pornillos O Proteins. 2017 Jul 6. doi: 10.1002/prot.25348. PMID:28681414<ref>PMID:28681414</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 5vzv" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Ubiquitin protein ligase|Ubiquitin protein ligase]]
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*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: RING-type E3 ubiquitin transferase]]
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[[Category: Dawidziak D]]
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[[Category: Dawidziak, D]]
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[[Category: Pornillos O]]
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[[Category: Pornillos, O]]
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[[Category: E3 ligase]]
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[[Category: Ring domain]]
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[[Category: Transferase]]
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Current revision

TRIM23 RING domain

PDB ID 5vzv

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