|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5vzv' size='340' side='right'caption='[[5vzv]], [[Resolution|resolution]] 1.81Å' scene=''> | | <StructureSection load='5vzv' size='340' side='right'caption='[[5vzv]], [[Resolution|resolution]] 1.81Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <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> | + | <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> |
| - | </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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.812Å</td></tr> |
| - | <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>
| + | <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> |
| - | <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> | + | <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> |
| - | <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> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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> | + | [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> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | 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.
| + | |
| - | | + | |
| - | 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>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 5vzv" style="background-color:#fffaf0;"></div>
| + | |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Ubiquitin protein ligase|Ubiquitin protein ligase]] | + | *[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: RING-type E3 ubiquitin transferase]]
| + | [[Category: Dawidziak D]] |
| - | [[Category: Dawidziak, D]] | + | [[Category: Pornillos O]] |
| - | [[Category: Pornillos, O]] | + | |
| - | [[Category: E3 ligase]]
| + | |
| - | [[Category: Ring domain]]
| + | |
| - | [[Category: Transferase]]
| + | |
