3w31 - Revision history

OCA at 12:47, 8 November 2023

OCA — Wed, 08 Nov 2023 12:47:47 GMT

←Older revision		Revision as of 12:47, 8 November 2023
Line 1:		Line 1:

	==Structual basis for the recognition of Ubc13 by the Shigella flexneri effector OspI==		==Structual basis for the recognition of Ubc13 by the Shigella flexneri effector OspI==
-	<StructureSection load='3w31' size='340' side='right'caption='[[3w31]]' scene=''>	+	<StructureSection load='3w31' size='340' side='right'caption='[[3w31]], [[Resolution\|resolution]] 2.96Å' 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=3W31 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W31 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3w31]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W31 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W31 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=3w31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w31 OCA], [https://pdbe.org/3w31 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w31 RCSB], [https://www.ebi.ac.uk/pdbsum/3w31 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w31 ProSAT]</span></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]] 2.96Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></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=3w31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w31 OCA], [https://pdbe.org/3w31 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w31 RCSB], [https://www.ebi.ac.uk/pdbsum/3w31 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w31 ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/Q8VSD5_SHIFL Q8VSD5_SHIFL]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Ubc13 is a ubiquitin-conjugating enzyme that plays a key role in the nuclear factor-kappaB signal transduction pathway in human diseases. The Shigella flexneri effector OspI affects inflammatory responses by catalyzing the deamidation of a specific glutamine residue at position 100 in Ubc13 during infection. This modification prevents the activation of the TNF (tumor necrosis factor) receptor-associated factor 6, leading to modulation of the diacylglycerol-CBM (CARD-Bcl10-Malt1) complex-TNF receptor-associated factor 6-nuclear factor-kappaB signaling pathway. To elucidate the structural basis of OspI function, we determined the crystal structures of the catalytically inert OspI C62A mutant and its complex with Ubc13 at resolutions of 3.0 and 2.96A, respectively. The structure of the OspI-Ubc13 complex revealed that the interacting surfaces between OspI and Ubc13 are a hydrophobic surface and a complementary charged surface. Furthermore, we predict that the complementary charged surface of OspI plays a key role in substrate specificity determination.
		+
		+	Structural Basis for the Recognition of Ubc13 by the Shigella flexneri Effector OspI.,Nishide A, Kim M, Takagi K, Himeno A, Sanada T, Sasakawa C, Mizushima T J Mol Biol. 2013 Aug 9;425(15):2623-31. doi: 10.1016/j.jmb.2013.02.037. Epub 2013, Mar 27. PMID:23542009<ref>PMID:23542009</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 3w31" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[3D structures of ubiquitin conjugating enzyme\|3D structures of ubiquitin conjugating enzyme]]		*[[3D structures of ubiquitin conjugating enzyme\|3D structures of ubiquitin conjugating enzyme]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
		+	[[Category: Shigella flexneri]]
	[[Category: Kim M]]		[[Category: Kim M]]
	[[Category: Mizushima T]]		[[Category: Mizushima T]]

OCA at 10:28, 31 August 2022

OCA — Wed, 31 Aug 2022 10:28:11 GMT

←Older revision		Revision as of 10:28, 31 August 2022
Line 1:		Line 1:

	==Structual basis for the recognition of Ubc13 by the Shigella flexneri effector OspI==		==Structual basis for the recognition of Ubc13 by the Shigella flexneri effector OspI==
-	<StructureSection load='3w31' size='340' side='right'caption='[[3w31]]~~, [[Resolution\|resolution]] 2.96Å~~' scene=''>	+	<StructureSection load='3w31' size='340' side='right'caption='[[3w31]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>~~[[3w31]] is a 2 chain structure.~~ Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W31 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W31 FirstGlance]. <br>	+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W31 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W31 FirstGlance]. <br>
-	</td></tr>~~<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>~~	+	</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=3w31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w31 OCA], [https://pdbe.org/3w31 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w31 RCSB], [https://www.ebi.ac.uk/pdbsum/3w31 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w31 ProSAT]</span></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3w30\|3w30]]</div></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>	+
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3w31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w31 OCA], [https://pdbe.org/3w31 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w31 RCSB], [https://www.ebi.ac.uk/pdbsum/3w31 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w31 ProSAT]</span></td></tr>	+
	</table>		</table>
-	== Function ==
-	[[https://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>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Ubc13 is a ubiquitin-conjugating enzyme that plays a key role in the nuclear factor-kappaB signal transduction pathway in human diseases. The Shigella flexneri effector OspI affects inflammatory responses by catalyzing the deamidation of a specific glutamine residue at position 100 in Ubc13 during infection. This modification prevents the activation of the TNF (tumor necrosis factor) receptor-associated factor 6, leading to modulation of the diacylglycerol-CBM (CARD-Bcl10-Malt1) complex-TNF receptor-associated factor 6-nuclear factor-kappaB signaling pathway. To elucidate the structural basis of OspI function, we determined the crystal structures of the catalytically inert OspI C62A mutant and its complex with Ubc13 at resolutions of 3.0 and 2.96A, respectively. The structure of the OspI-Ubc13 complex revealed that the interacting surfaces between OspI and Ubc13 are a hydrophobic surface and a complementary charged surface. Furthermore, we predict that the complementary charged surface of OspI plays a key role in substrate specificity determination.
-
-	Structural Basis for the Recognition of Ubc13 by the Shigella flexneri Effector OspI.,Nishide A, Kim M, Takagi K, Himeno A, Sanada T, Sasakawa C, Mizushima T J Mol Biol. 2013 Aug 9;425(15):2623-31. doi: 10.1016/j.jmb.2013.02.037. Epub 2013, Mar 27. PMID:23542009<ref>PMID:23542009</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 3w31" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[3D structures of ubiquitin conjugating enzyme\|3D structures of ubiquitin conjugating enzyme]]		*[[3D structures of ubiquitin conjugating enzyme\|3D structures of ubiquitin conjugating enzyme]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Ubiquitin--protein ligase]]~~	+	[[Category: Kim M]]
-	[[Category: Kim, M]]	+	[[Category: Mizushima T]]
-	[[Category: Mizushima, T]]	+	[[Category: Nishide A]]
-	[[Category: Nishide, A]]	+	[[Category: Sasakawa C]]
-	[[Category: Sasakawa, C]]	+	[[Category: Takagi K]]
-	[[Category: Takagi, K]]	+
-	~~[[Category: Deamidation]]~~	+
-	~~[[Category: Effector]]~~	+
-	~~[[Category: Immune system]]~~	+
-	~~[[Category: Type 3 secretion system~~]]	+

OCA at 04:56, 25 August 2022

OCA — Thu, 25 Aug 2022 04:56:37 GMT

←Older revision		Revision as of 04:56, 25 August 2022
Line 3:		Line 3:
	<StructureSection load='3w31' size='340' side='right'caption='[[3w31]], [[Resolution\|resolution]] 2.96Å' scene=''>		<StructureSection load='3w31' size='340' side='right'caption='[[3w31]], [[Resolution\|resolution]] 2.96Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3w31]] is a 2 chain structure ~~with sequence from [https://en.wikipedia.org/wiki/"shigella_paradysenteriae"_weldin_1927 "shigella paradysenteriae" weldin 1927] and [https://en.wikipedia.org/wiki/Human Human]~~. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W31 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W31 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3w31]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W31 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W31 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3w30\|3w30]]</div></td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3w30\|3w30]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ORF169b, CP0209 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=623 "Shigella paradysenteriae" Weldin 1927]), UBE2N, BLU ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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>		<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>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3w31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w31 OCA], [https://pdbe.org/3w31 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w31 RCSB], [https://www.ebi.ac.uk/pdbsum/3w31 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w31 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=3w31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w31 OCA], [https://pdbe.org/3w31 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w31 RCSB], [https://www.ebi.ac.uk/pdbsum/3w31 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w31 ProSAT]</span></td></tr>
Line 28:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Shigella paradysenteriae weldin 1927]]
-	[[Category: Human]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Ubiquitin--protein ligase]]		[[Category: Ubiquitin--protein ligase]]

OCA at 05:20, 3 August 2022

OCA — Wed, 03 Aug 2022 05:20:39 GMT

←Older revision		Revision as of 05:20, 3 August 2022
Line 1:		Line 1:

	==Structual basis for the recognition of Ubc13 by the Shigella flexneri effector OspI==		==Structual basis for the recognition of Ubc13 by the Shigella flexneri effector OspI==
-	<StructureSection load='3w31' size='340' side='right' caption='[[3w31]], [[Resolution\|resolution]] 2.96Å' scene=''>	+	<StructureSection load='3w31' size='340' side='right'caption='[[3w31]], [[Resolution\|resolution]] 2.96Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3w31]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"shigella_paradysenteriae"_weldin_1927 "shigella paradysenteriae" weldin 1927] and [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W31 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3W31 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3w31]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"shigella_paradysenteriae"_weldin_1927 "shigella paradysenteriae" weldin 1927] and [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W31 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W31 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3w30\|3w30]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3w30\|3w30]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ORF169b, CP0209 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=623 "Shigella paradysenteriae" Weldin 1927]), UBE2N, BLU ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ORF169b, CP0209 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=623 "Shigella paradysenteriae" Weldin 1927]), UBE2N, BLU ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] </span></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>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3w31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w31 OCA], [~~http~~://pdbe.org/3w31 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3w31 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3w31 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3w31 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=3w31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w31 OCA], [https://pdbe.org/3w31 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w31 RCSB], [https://www.ebi.ac.uk/pdbsum/3w31 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w31 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/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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 23:

	==See Also==		==See Also==
-	*[[~~Ubiquitin~~ conjugating enzyme\|~~Ubiquitin~~ conjugating enzyme]]	+	*[[3D structures of ubiquitin conjugating enzyme\|3D structures of ubiquitin conjugating enzyme]]
	== References ==		== References ==
	<references/>		<references/>
Line 30:		Line 30:
	[[Category: Shigella paradysenteriae weldin 1927]]		[[Category: Shigella paradysenteriae weldin 1927]]
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Ubiquitin--protein ligase]]		[[Category: Ubiquitin--protein ligase]]
	[[Category: Kim, M]]		[[Category: Kim, M]]

OCA at 15:51, 5 August 2016

OCA — Fri, 05 Aug 2016 15:51:26 GMT

←Older revision		Revision as of 15:51, 5 August 2016
Line 1:		Line 1:
		+
	==Structual basis for the recognition of Ubc13 by the Shigella flexneri effector OspI==		==Structual basis for the recognition of Ubc13 by the Shigella flexneri effector OspI==
	<StructureSection load='3w31' size='340' side='right' caption='[[3w31]], [[Resolution\|resolution]] 2.96Å' scene=''>		<StructureSection load='3w31' size='340' side='right' caption='[[3w31]], [[Resolution\|resolution]] 2.96Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3w31]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~] and [http://en.wikipedia.org/wiki/~~Shigella_flexneri Shigella flexneri~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W31 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3W31 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3w31]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"shigella_paradysenteriae"_weldin_1927 "shigella paradysenteriae" weldin 1927] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W31 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3W31 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3w30\|3w30]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3w30\|3w30]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ORF169b, CP0209 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=623 Shigella ~~flexneri~~]), UBE2N, BLU ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ORF169b, CP0209 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=623 "Shigella paradysenteriae" Weldin 1927]), UBE2N, BLU ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3w31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w31 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3w31 RCSB], [http://www.ebi.ac.uk/pdbsum/3w31 PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3w31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w31 OCA], [http://pdbe.org/3w31 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3w31 RCSB], [http://www.ebi.ac.uk/pdbsum/3w31 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3w31 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 3w31" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 26:		Line 28:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Shigella paradysenteriae weldin 1927]]
-	[[Category: ~~Shigella flexneri~~]]	+	[[Category: Human]]
	[[Category: Ubiquitin--protein ligase]]		[[Category: Ubiquitin--protein ligase]]
	[[Category: Kim, M]]		[[Category: Kim, M]]

OCA at 03:44, 25 December 2014

OCA — Thu, 25 Dec 2014 03:44:52 GMT

←Older revision		Revision as of 03:44, 25 December 2014
Line 9:		Line 9:
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3w31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w31 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3w31 RCSB], [http://www.ebi.ac.uk/pdbsum/3w31 PDBsum]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3w31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w31 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3w31 RCSB], [http://www.ebi.ac.uk/pdbsum/3w31 PDBsum]</span></td></tr>
	</table>		</table>
		+	== 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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 06:43, 21 December 2014

OCA — Sun, 21 Dec 2014 06:43:29 GMT

←Older revision		Revision as of 06:43, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3w31\| PDB=3w31 \| SCENE= }}~~	+	==Structual basis for the recognition of Ubc13 by the Shigella flexneri effector OspI==
-	===Structual basis for the recognition of Ubc13 by the Shigella flexneri effector OspI===	+	<StructureSection load='3w31' size='340' side='right' caption='[[3w31]], [[Resolution\|resolution]] 2.96Å' scene=''>
-	~~{{ABSTRACT_PUBMED_23542009}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3w31]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W31 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3W31 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3w30\|3w30]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ORF169b, CP0209 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=623 Shigella flexneri]), UBE2N, BLU ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] </span></td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3w31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w31 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3w31 RCSB], [http://www.ebi.ac.uk/pdbsum/3w31 PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Ubc13 is a ubiquitin-conjugating enzyme that plays a key role in the nuclear factor-kappaB signal transduction pathway in human diseases. The Shigella flexneri effector OspI affects inflammatory responses by catalyzing the deamidation of a specific glutamine residue at position 100 in Ubc13 during infection. This modification prevents the activation of the TNF (tumor necrosis factor) receptor-associated factor 6, leading to modulation of the diacylglycerol-CBM (CARD-Bcl10-Malt1) complex-TNF receptor-associated factor 6-nuclear factor-kappaB signaling pathway. To elucidate the structural basis of OspI function, we determined the crystal structures of the catalytically inert OspI C62A mutant and its complex with Ubc13 at resolutions of 3.0 and 2.96A, respectively. The structure of the OspI-Ubc13 complex revealed that the interacting surfaces between OspI and Ubc13 are a hydrophobic surface and a complementary charged surface. Furthermore, we predict that the complementary charged surface of OspI plays a key role in substrate specificity determination.

-	~~==Function==~~	+	Structural Basis for the Recognition of Ubc13 by the Shigella flexneri Effector OspI.,Nishide A, Kim M, Takagi K, Himeno A, Sanada T, Sasakawa C, Mizushima T J Mol Biol. 2013 Aug 9;425(15):2623-31. doi: 10.1016/j.jmb.2013.02.037. Epub 2013, Mar 27. PMID:23542009<ref>PMID:23542009</ref>
-	~~[[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>	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[3w31]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens] and [http://en~~.~~wikipedia.org~~/~~wiki/Shigella_flexneri Shigella flexneri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W31 OCA].~~	+	</div>

	==See Also==		==See Also==
	*[[Ubiquitin conjugating enzyme\|Ubiquitin conjugating enzyme]]		*[[Ubiquitin conjugating enzyme\|Ubiquitin conjugating enzyme]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:023542009</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Shigella flexneri]]		[[Category: Shigella flexneri]]
	[[Category: Ubiquitin--protein ligase]]		[[Category: Ubiquitin--protein ligase]]
-	[[Category: Kim, M.]]	+	[[Category: Kim, M]]
-	[[Category: Mizushima, T.]]	+	[[Category: Mizushima, T]]
-	[[Category: Nishide, A.]]	+	[[Category: Nishide, A]]
-	[[Category: Sasakawa, C.]]	+	[[Category: Sasakawa, C]]
-	[[Category: Takagi, K.]]	+	[[Category: Takagi, K]]
	[[Category: Deamidation]]		[[Category: Deamidation]]
	[[Category: Effector]]		[[Category: Effector]]
	[[Category: Immune system]]		[[Category: Immune system]]
	[[Category: Type 3 secretion system]]		[[Category: Type 3 secretion system]]

OCA at 04:25, 18 July 2013

OCA — Thu, 18 Jul 2013 04:25:41 GMT

←Older revision		Revision as of 04:25, 18 July 2013
Line 1:		Line 1:
	{{STRUCTURE_3w31\| PDB=3w31 \| SCENE= }}		{{STRUCTURE_3w31\| PDB=3w31 \| SCENE= }}
	===Structual basis for the recognition of Ubc13 by the Shigella flexneri effector OspI===		===Structual basis for the recognition of Ubc13 by the Shigella flexneri effector OspI===
		+	{{ABSTRACT_PUBMED_23542009}}

	==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>	+	[[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>

	==About this Structure==		==About this Structure==
	[[3w31]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W31 OCA].		[[3w31]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W31 OCA].
		+
		+	==See Also==
		+	*[[Ubiquitin conjugating enzyme\|Ubiquitin conjugating enzyme]]

	==Reference==		==Reference==
-	<references group="xtra"/><references/>	+	<ref group="xtra">PMID:023542009</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Shigella flexneri]]		[[Category: Shigella flexneri]]

OCA at 08:53, 27 March 2013

OCA — Wed, 27 Mar 2013 08:53:35 GMT

←Older revision		Revision as of 08:53, 27 March 2013
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_3w31\| PDB=3w31 \| SCENE= }}
		+	===Structual basis for the recognition of Ubc13 by the Shigella flexneri effector OspI===

-	The ~~entry 3w31~~ is ~~ON HOLD until Paper Publication~~	+	==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>

-	~~Authors~~: ~~Nishide, A~~.~~, Kim, M~~.~~, Takagi, K~~.~~, Sasakawa, C~~.~~, Mizushima, T~~.	+	==About this Structure==
		+	[[3w31]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W31 OCA].

-	~~Description~~: ~~Structual basis for the recognition of Ubc13 by the~~ Shigella flexneri ~~effector OspI~~	+	==Reference==
		+	<references group="xtra"/><references/>
		+	[[Category: Homo sapiens]]
		+	[[Category: Shigella flexneri]]
		+	[[Category: Ubiquitin--protein ligase]]
		+	[[Category: Kim, M.]]
		+	[[Category: Mizushima, T.]]
		+	[[Category: Nishide, A.]]
		+	[[Category: Sasakawa, C.]]
		+	[[Category: Takagi, K.]]
		+	[[Category: Deamidation]]
		+	[[Category: Effector]]
		+	[[Category: Immune system]]
		+	[[Category: Type 3 secretion system]]

OCA at 16:01, 20 March 2013

OCA — Wed, 20 Mar 2013 16:01:07 GMT

←Older revision		Revision as of 16:01, 20 March 2013
Line 5:		Line 5:
	Authors: Nishide, A., Kim, M., Takagi, K., Sasakawa, C., Mizushima, T.		Authors: Nishide, A., Kim, M., Takagi, K., Sasakawa, C., Mizushima, T.

-	Description: ~~Effector protein 01~~	+	Description: Structual basis for the recognition of Ubc13 by the Shigella flexneri effector OspI