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| | <StructureSection load='7bxf' size='340' side='right'caption='[[7bxf]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='7bxf' size='340' side='right'caption='[[7bxf]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7bxf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Legph Legph]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BXF OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7BXF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7bxf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Legionella_pneumophila_subsp._pneumophila_str._Philadelphia_1 Legionella pneumophila subsp. pneumophila str. Philadelphia 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BXF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BXF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PR:PRASEODYMIUM+ION'>PR</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]] 2.7Å</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]), lpg2149 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272624 LEGPH])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PR:PRASEODYMIUM+ION'>PR</scene></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=7bxf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bxf OCA], [http://pdbe.org/7bxf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7bxf RCSB], [http://www.ebi.ac.uk/pdbsum/7bxf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7bxf ProSAT]</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=7bxf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bxf OCA], [https://pdbe.org/7bxf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bxf RCSB], [https://www.ebi.ac.uk/pdbsum/7bxf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bxf ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [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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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Legph]] | + | [[Category: Legionella pneumophila subsp. pneumophila str. Philadelphia 1]] |
| - | [[Category: Gao, P]] | + | [[Category: Gao P]] |
| - | [[Category: Deubiquitination]]
| + | |
| - | [[Category: Lpg2149]]
| + | |
| - | [[Category: Mavc]]
| + | |
| - | [[Category: Mvca]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Ube2n]]
| + | |
| - | [[Category: Ubiquitination]]
| + | |
| Structural highlights
Function
Q5ZTL3_LEGPH
Publication Abstract from PubMed
The bacterial effector MavC catalyzes non-canonical ubiquitination of host E2 enzyme UBE2N without engaging any of the conventional ubiquitination machinery, thereby abolishing UBE2N's function in forming K63-linked ubiquitin (Ub) chains and dampening NF-small ka, CyrillicB signaling. We now report the structures of MavC in complex with conjugated UBE2N~Ub and an inhibitor protein Lpg2149, as well as the structure of its ortholog, MvcA, bound to Lpg2149. Recognition of UBE2N and Ub depends on several unique features of MavC, which explains the inability of MvcA to catalyze ubiquitination. Unexpectedly, MavC and MvcA also possess deubiquitinase activity against MavC-mediated ubiquitination, highlighting MavC as a unique enzyme possessing deamidation, ubiquitination, and deubiquitination activities. Further, Lpg2149 directly binds and inhibits both MavC and MvcA by disrupting the interactions between enzymes and Ub. These results provide detailed insights into catalysis and regulation of MavC-type enzymes and the molecular mechanisms of this non-canonical ubiquitination machinery.
Insights into catalysis and regulation of non-canonical ubiquitination and deubiquitination by bacterial deamidase effectors.,Wang Y, Zhan Q, Wang X, Li P, Liu S, Gao G, Gao P Nat Commun. 2020 Jun 2;11(1):2751. doi: 10.1038/s41467-020-16587-w. PMID:32488130[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wang Y, Zhan Q, Wang X, Li P, Liu S, Gao G, Gao P. Insights into catalysis and regulation of non-canonical ubiquitination and deubiquitination by bacterial deamidase effectors. Nat Commun. 2020 Jun 2;11(1):2751. doi: 10.1038/s41467-020-16587-w. PMID:32488130 doi:http://dx.doi.org/10.1038/s41467-020-16587-w
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