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| | <StructureSection load='6jky' size='340' side='right'caption='[[6jky]], [[Resolution|resolution]] 2.45Å' scene=''> | | <StructureSection load='6jky' size='340' side='right'caption='[[6jky]], [[Resolution|resolution]] 2.45Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6jky]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human], [http://en.wikipedia.org/wiki/Legph Legph] and [http://en.wikipedia.org/wiki/Schistosoma_margrebowiei Schistosoma margrebowiei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JKY OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6JKY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6jky]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Legionella_pneumophila_subsp._pneumophila_str._Philadelphia_1 Legionella pneumophila subsp. pneumophila str. Philadelphia 1] and [https://en.wikipedia.org/wiki/Schistosoma_margrebowiei Schistosoma margrebowiei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JKY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JKY FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lpg2148 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272624 LEGPH]), UBE2N ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), SMRZ_LOCUS12712 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=48269 Schistosoma margrebowiei])</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]] 2.454Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/E2_ubiquitin-conjugating_enzyme E2 ubiquitin-conjugating enzyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.23 2.3.2.23] </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=6jky FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jky OCA], [https://pdbe.org/6jky PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jky RCSB], [https://www.ebi.ac.uk/pdbsum/6jky PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jky ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6jky FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jky OCA], [http://pdbe.org/6jky PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jky RCSB], [http://www.ebi.ac.uk/pdbsum/6jky PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jky ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/UBE2N_HUMAN UBE2N_HUMAN]] The UBE2V1-UBE2N and UBE2V2-UBE2N heterodimers catalyze the synthesis of non-canonical 'Lys-63'-linked polyubiquitin chains. This type of polyubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. Acts together with the E3 ligases, HLTF and SHPRH, in the 'Lys-63'-linked poly-ubiquitination of PCNA upon genotoxic stress, which is required for DNA repair. Appears to act together with E3 ligase RNF5 in the 'Lys-63'-linked polyubiquitination of JKAMP thereby regulating JKAMP function by decreasing its association with components of the proteasome and ERAD. Promotes TRIM5 capsid-specific restriction activity and the UBE2V1-UBE2N heterodimer acts in concert with TRIM5 to generate 'Lys-63'-linked polyubiquitin chains which activate the MAP3K7/TAK1 complex which in turn results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes (By similarity).<ref>PMID:10089880</ref> <ref>PMID:14562038</ref> <ref>PMID:19269966</ref> <ref>PMID:20061386</ref> <ref>PMID:21512573</ref> | + | [https://www.uniprot.org/uniprot/Q5ZTL3_LEGPH Q5ZTL3_LEGPH] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6jky" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6jky" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[3D structures of ubiquitin|3D structures of ubiquitin]] |
| | + | *[[3D structures of ubiquitin conjugating enzyme|3D structures of ubiquitin conjugating enzyme]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: E2 ubiquitin-conjugating enzyme]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Human]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Legph]] | + | [[Category: Legionella pneumophila subsp. pneumophila str. Philadelphia 1]] |
| | [[Category: Schistosoma margrebowiei]] | | [[Category: Schistosoma margrebowiei]] |
| - | [[Category: Guan, H]] | + | [[Category: Guan H]] |
| - | [[Category: Ouyang, S Y]] | + | [[Category: Ouyang SY]] |
| - | [[Category: Legionella pneumophila effect factor complex]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| Structural highlights
Function
Q5ZTL3_LEGPH
Publication Abstract from PubMed
The Legionella pneumophila effector MavC induces ubiquitination of the E2 ubiquitin-conjugating enzyme UBE2N by transglutamination, thereby abolishing its function in the synthesis of K63 -type polyubiquitin chains. The inhibition of UBE2N activity creates a conundrum because this E2 enzyme is important in multiple signaling pathways, including some that are important for intracellular L. pneumophila replication. Here, we show that prolonged inhibition of UBE2N activity by MavC restricts intracellular bacterial replication and that the activity of UBE2N is restored by MvcA, an ortholog of MavC (50% identity) with ubiquitin deamidase activity. MvcA functions to deubiquitinate UBE2N-Ub using the same catalytic triad required for its deamidase activity. Structural analysis of the MvcA-UBE2N-Ub complex reveals a crucial role of the insertion domain in MvcA in substrate recognition. Our study establishes a deubiquitination mechanism catalyzed by a deamidase, which, together with MavC, imposes temporal regulation of the activity of UBE2N during L. pneumophila infection.
Legionella pneumophila regulates the activity of UBE2N by deamidase-mediated deubiquitination.,Gan N, Guan H, Huang Y, Yu T, Fu J, Nakayasu ES, Puvar K, Das C, Wang D, Ouyang S, Luo ZQ EMBO J. 2020 Feb 17;39(4):e102806. doi: 10.15252/embj.2019102806. Epub 2019 Dec, 11. PMID:31825121[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gan N, Guan H, Huang Y, Yu T, Fu J, Nakayasu ES, Puvar K, Das C, Wang D, Ouyang S, Luo ZQ. Legionella pneumophila regulates the activity of UBE2N by deamidase-mediated deubiquitination. EMBO J. 2020 Feb 17;39(4):e102806. doi: 10.15252/embj.2019102806. Epub 2019 Dec, 11. PMID:31825121 doi:http://dx.doi.org/10.15252/embj.2019102806
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