6m2d

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==MUL1-RING domain==
==MUL1-RING domain==
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<StructureSection load='6m2d' size='340' side='right'caption='[[6m2d]]' scene=''>
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<StructureSection load='6m2d' size='340' side='right'caption='[[6m2d]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M2D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6M2D FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6m2d]] is a 6 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=6M2D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6M2D FirstGlance]. <br>
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</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=6m2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m2d OCA], [https://pdbe.org/6m2d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6m2d RCSB], [https://www.ebi.ac.uk/pdbsum/6m2d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6m2d ProSAT]</span></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]] 1.795&#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=SO4:SULFATE+ION'>SO4</scene>, <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=6m2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m2d OCA], [https://pdbe.org/6m2d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6m2d RCSB], [https://www.ebi.ac.uk/pdbsum/6m2d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6m2d ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MUL1_HUMAN MUL1_HUMAN] Exhibits weak E3 ubiquitin-protein ligase activity (PubMed:18591963, PubMed:19407830, PubMed:22410793). E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates (PubMed:18591963, PubMed:19407830, PubMed:22410793). Can ubiquitinate AKT1 preferentially at 'Lys-284' involving 'Lys-48'-linked polyubiquitination and seems to be involved in regulation of Akt signaling by targeting phosphorylated Akt to proteosomal degradation (PubMed:22410793). Proposed to preferentially act as a SUMO E3 ligase at physiological concentrations (PubMed:19407830). Plays a role in the control of mitochondrial morphology by promoting mitochondrial fragmentation, and influences mitochondrial localization (PubMed:19407830, PubMed:18207745, PubMed:18213395). Likely to promote mitochondrial fission through negatively regulating the mitochondrial fusion proteins MFN1 and MFN2, acting in a pathway that is parallel to the PRKN/PINK1 regulatory pathway (PubMed:24898855). May also be involved in the sumoylation of the membrane fission protein DNM1L (PubMed:18207745, PubMed:19407830). Inhibits cell growth (PubMed:18591963, PubMed:22410793). When overexpressed, activates JNK through MAP3K7/TAK1 and induces caspase-dependent apoptosis (PubMed:23399697). Involved in the modulation of innate immune defense against viruses by inhibiting DDX58-dependent antiviral response (PubMed:23399697). Can mediate DDX58 sumoylation and disrupt its polyubiquitination (PubMed:23399697).<ref>PMID:18207745</ref> <ref>PMID:18213395</ref> <ref>PMID:18591963</ref> <ref>PMID:19407830</ref> <ref>PMID:22410793</ref> <ref>PMID:23399697</ref> <ref>PMID:24898855</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The RING domain of MUL1 (RINGMUL1 ) alone mediates ubiquitylation of the p53-transactivation domain (TADp53 ). To elucidate the mechanism underlying the simultaneous recruitment of UBE2D2 and the substrate TADp53 by RINGMUL1 , we determined the complex structure of RINGMUL1 :UBE2D2 and studied the interaction between RINGMUL1 and TADp53 in the presence of UBE2D2-UB thioester (UBE2D2~UB) mimetics. The RINGMUL1 -binding induced the closed conformation of UBE2D2(S22R/C85S) -UB(K48R) oxyester (UBE2D2(RS) -UB(R) OE ), and strongly accelerated its hydrolysis, which was suppressed by the additional N77A-mutation of UBE2D2. Interestingly, UBE2D2(S22R/N77A/C85S) -UB(K48R) oxyester (UBE2D2(RAS) -UB(R) OE ) already formed a closed conformation in the absence of RINGMUL1 . Although TADp53 exhibited weak binding for RINGMUL1 or UBE2D2 alone, its binding affinity was enhanced and even further for RINGMUL1 :UBE2D2 and RINGMUL1 :UBE2D2(RAS) -UB(R) OE , respectively. The recognition of TADp53 by RINGMUL1 as a complex with UBE2D2~UB is related to the multivalency of the binding events and underlies the ability of RINGMUL1 to ubiquitylate the intrinsically disordered protein, TADp53 .
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MUL1-RING recruits the substrate, p53-TAD as a complex with UBE2D2-UB conjugate.,Lee MS, Lee SO, Choi J, Ryu M, Lee MK, Kim JH, Hwang E, Lee CK, Chi SW, Ryu KS FEBS J. 2022 Jan 19. doi: 10.1111/febs.16360. PMID:35048531<ref>PMID:35048531</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 6m2d" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Chi S-W]]
[[Category: Chi S-W]]
[[Category: Lee SO]]
[[Category: Lee SO]]
[[Category: Ryu KS]]
[[Category: Ryu KS]]

Current revision

MUL1-RING domain

PDB ID 6m2d

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