6y5p
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==RING-DTC domain of Deltex1 bound to NAD== | |
| + | <StructureSection load='6y5p' size='340' side='right'caption='[[6y5p]], [[Resolution|resolution]] 1.74Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Y5P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Y5P FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.74Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6y5p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6y5p OCA], [https://pdbe.org/6y5p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6y5p RCSB], [https://www.ebi.ac.uk/pdbsum/6y5p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6y5p ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Cellular cross-talk between ubiquitination and other posttranslational modifications contributes to the regulation of numerous processes. One example is ADP-ribosylation of the carboxyl terminus of ubiquitin by the E3 DTX3L/ADP-ribosyltransferase PARP9 heterodimer, but the mechanism remains elusive. Here, we show that independently of PARP9, the conserved carboxyl-terminal RING and DTC (Deltex carboxyl-terminal) domains of DTX3L and other human Deltex proteins (DTX1 to DTX4) catalyze ADP-ribosylation of ubiquitin's Gly(76) Structural studies reveal a hitherto unknown function of the DTC domain in binding NAD(+) Deltex RING domain recruits E2 thioesterified with ubiquitin and juxtaposes it with NAD(+) bound to the DTC domain to facilitate ADP-ribosylation of ubiquitin. This ubiquitin modification prevents its activation but is reversed by the linkage nonspecific deubiquitinases. Our study provides mechanistic insights into ADP-ribosylation of ubiquitin by Deltex E3s and will enable future studies directed at understanding the increasingly complex network of ubiquitin cross-talk. | ||
| - | + | Structural insights into ADP-ribosylation of ubiquitin by Deltex family E3 ubiquitin ligases.,Chatrin C, Gabrielsen M, Buetow L, Nakasone MA, Ahmed SF, Sumpton D, Sibbet GJ, Smith BO, Huang DT Sci Adv. 2020 Sep 18;6(38). pii: 6/38/eabc0418. doi: 10.1126/sciadv.abc0418., Print 2020 Sep. PMID:32948590<ref>PMID:32948590</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6y5p" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Buetow L]] | ||
| + | [[Category: Gabrielsen M]] | ||
| + | [[Category: Huang DT]] | ||
Current revision
RING-DTC domain of Deltex1 bound to NAD
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