7bol
From Proteopedia
(Difference between revisions)
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==ubiquitin-conjugating enzyme, Ube2D2== | ==ubiquitin-conjugating enzyme, Ube2D2== | ||
- | <StructureSection load='7bol' size='340' side='right'caption='[[7bol]]' scene=''> | + | <StructureSection load='7bol' size='340' side='right'caption='[[7bol]], [[Resolution|resolution]] 1.80Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BOL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BOL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7bol]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BOL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BOL FirstGlance]. <br> |
- | </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=7bol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bol OCA], [https://pdbe.org/7bol PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bol RCSB], [https://www.ebi.ac.uk/pdbsum/7bol PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bol ProSAT]</span></td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">UBE2D2, PUBC1, UBC4, UBC5B, UBCH4, UBCH5B ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=7bol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bol OCA], [https://pdbe.org/7bol PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bol RCSB], [https://www.ebi.ac.uk/pdbsum/7bol PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bol ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [[https://www.uniprot.org/uniprot/UB2D2_HUMAN UB2D2_HUMAN]] Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and autoubiquitination of STUB1 and TRAF6. Involved in the signal-induced conjugation and subsequent degradation of NFKBIA, FBXW2-mediated GCM1 ubiquitination and degradation, MDM2-dependent degradation of p53/TP53 and the activation of MAVS in the mitochondria by DDX58/RIG-I in response to viral infection. Essential for viral activation of IRF3.<ref>PMID:10329681</ref> <ref>PMID:15280377</ref> <ref>PMID:18042044</ref> <ref>PMID:18703417</ref> <ref>PMID:18359941</ref> <ref>PMID:19854139</ref> <ref>PMID:20403326</ref> <ref>PMID:20061386</ref> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | 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 . | ||
+ | |||
+ | 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> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 7bol" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
+ | [[Category: Human]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Chi S | + | [[Category: Chi, S W]] |
- | [[Category: Lee | + | [[Category: Lee, S O]] |
- | [[Category: Ryu | + | [[Category: Ryu, K S]] |
+ | [[Category: Structural protein]] | ||
+ | [[Category: Ube2d2]] | ||
+ | [[Category: Ubiquitin-conjugating enzyme]] |
Revision as of 03:03, 21 April 2022
ubiquitin-conjugating enzyme, Ube2D2
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