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| | <StructureSection load='3sy2' size='340' side='right'caption='[[3sy2]], [[Resolution|resolution]] 3.27Å' scene=''> | | <StructureSection load='3sy2' size='340' side='right'caption='[[3sy2]], [[Resolution|resolution]] 3.27Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3sy2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_typhimurium"_loeffler_1892 "bacillus typhimurium" loeffler 1892] and [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SY2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SY2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3sy2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SY2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SY2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 3.27Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sopA, STM2066 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 "Bacillus typhimurium" Loeffler 1892]), UBE2L3, UBCE7, UBCH7 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] </span></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=3sy2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sy2 OCA], [https://pdbe.org/3sy2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sy2 RCSB], [https://www.ebi.ac.uk/pdbsum/3sy2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sy2 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=3sy2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sy2 OCA], [https://pdbe.org/3sy2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sy2 RCSB], [https://www.ebi.ac.uk/pdbsum/3sy2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sy2 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/SOPA_SALTY SOPA_SALTY]] Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin ligase that interferes with host's ubiquitination pathway. Required for inducing polymorphonuclear leukocytes migration across the intestinal epithelium. Preferentially uses host UBE2D1 (UBCH5A), UBE2D2 (UBCH5B) and UBE2L3 (UBCH7) as E2 ubiquitin-conjugating enzymes.<ref>PMID:17076670</ref> <ref>PMID:18066077</ref> [[https://www.uniprot.org/uniprot/UB2L3_HUMAN UB2L3_HUMAN]] Ubiquitin-conjugating enzyme E2 that specifically acts with HECT-type and RBR family E3 ubiquitin-protein ligases. Does not function with most RING-containing E3 ubiquitin-protein ligases because it lacks intrinsic E3-independent reactivity with lysine: in contrast, it has activity with the RBR family E3 enzymes, such as PARK2 and ARIH1, that function like function like RING-HECT hybrids. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'-linked polyubiquitination. Involved in the selective degradation of short-lived and abnormal proteins. Down-regulated during the S-phase it is involved in progression through the cell cycle. Regulates nuclear hormone receptors transcriptional activity. May play a role in myelopoiesis.<ref>PMID:10888878</ref> <ref>PMID:15367689</ref> <ref>PMID:17003263</ref> <ref>PMID:19340006</ref> <ref>PMID:18946090</ref> <ref>PMID:20061386</ref> <ref>PMID:21532592</ref>
| + | [https://www.uniprot.org/uniprot/SOPA_SALTY SOPA_SALTY] Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin ligase that interferes with host's ubiquitination pathway. Required for inducing polymorphonuclear leukocytes migration across the intestinal epithelium. Preferentially uses host UBE2D1 (UBCH5A), UBE2D2 (UBCH5B) and UBE2L3 (UBCH7) as E2 ubiquitin-conjugating enzymes.<ref>PMID:17076670</ref> <ref>PMID:18066077</ref> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | In eukaryotes, ubiquitination is an important posttranslational process achieved through a cascade of ubiquitin-activating (E1), conjugating (E2), and ligase (E3) enzymes. Many pathogenic bacteria deliver virulence factors into the host cell that function as E3 ligases. How these bacterial "Trojan horses" integrate into the eukaryotic ubiquitin system has remained a mystery. Here we report crystal structures of two bacterial E3s, Salmonella SopA and Escherichia coli NleL, both in complex with human E2 UbcH7. These structures represent two distinct conformational states of the bacterial E3s, supporting the necessary structural rearrangements associated with ubiquitin transfer. The E2-interacting surface of SopA and NleL has little similarity to those of eukaryotic E3s. However, both bacterial E3s bind to the canonical surface of E2 that normally interacts with eukaryotic E3s. Furthermore, we show that a glutamate residue on E3 is involved in catalyzing ubiquitin transfer from E3 to the substrate, but not from E2 to E3. Together, these results provide mechanistic insights into the ubiquitin pathway and a framework for understanding molecular mimicry in bacterial pathogenesis.
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| - | Crystal structures of two bacterial HECT-like E3 ligases in complex with a human E2 reveal atomic details of pathogen-host interactions.,Lin DY, Diao J, Chen J Proc Natl Acad Sci U S A. 2012 Feb 7;109(6):1925-30. Epub 2012 Jan 23. PMID:22308380<ref>PMID:22308380</ref>
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| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 3sy2" style="background-color:#fffaf0;"></div>
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| | ==See Also== | | ==See Also== |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus typhimurium loeffler 1892]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Human]]
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ubiquitin--protein ligase]] | + | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium]] |
| - | [[Category: Chen, J]] | + | [[Category: Chen J]] |
| - | [[Category: Diao, J]] | + | [[Category: Diao J]] |
| - | [[Category: Lin, D Y]] | + | [[Category: Lin DY]] |
| - | [[Category: E2 ubiquitin conjugating enzyme]]
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| - | [[Category: Effector protein]]
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| - | [[Category: Hect domain]]
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| - | [[Category: Hect e3]]
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| - | [[Category: Hect e3 ubiquitin ligase]]
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| - | [[Category: Ligase-signaling protein complex]]
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| - | [[Category: Pentapeptide]]
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| - | [[Category: Protein-protein complex]]
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| - | [[Category: Ubiquitin]]
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| - | [[Category: Ubiquitin transfer]]
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| - | [[Category: Ubiquitination]]
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