4v3k - Revision history

OCA at 10:40, 10 January 2024

OCA — Wed, 10 Jan 2024 10:40:01 GMT

←Older revision		Revision as of 10:40, 10 January 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4v3k]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V3K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V3K FirstGlance]. <br>		<table><tr><td colspan='2'>[[4v3k]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V3K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V3K FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.04Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4v3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v3k OCA], [https://pdbe.org/4v3k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v3k RCSB], [https://www.ebi.ac.uk/pdbsum/4v3k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v3k 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=4v3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v3k OCA], [https://pdbe.org/4v3k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v3k RCSB], [https://www.ebi.ac.uk/pdbsum/4v3k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v3k ProSAT]</span></td></tr>
	</table>		</table>

OCA at 08:01, 29 March 2023

OCA — Wed, 29 Mar 2023 08:01:51 GMT

←Older revision		Revision as of 08:01, 29 March 2023
Line 3:		Line 3:
	<StructureSection load='4v3k' size='340' side='right'caption='[[4v3k]], [[Resolution\|resolution]] 2.04Å' scene=''>		<StructureSection load='4v3k' size='340' side='right'caption='[[4v3k]], [[Resolution\|resolution]] 2.04Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4v3k]] is a 6 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V3K OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4V3K FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4v3k]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V3K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V3K FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4v3l\|4v3l]]</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=4v3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v3k OCA], [https://pdbe.org/4v3k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v3k RCSB], [https://www.ebi.ac.uk/pdbsum/4v3k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v3k ProSAT]</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=4v3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v3k OCA], [~~http~~://pdbe.org/4v3k PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4v3k RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4v3k PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4v3k ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://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> [[http://www.uniprot.org/uniprot/UBC_HUMAN UBC_HUMAN]] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.<ref>PMID:16543144</ref> <ref>PMID:19754430</ref>	+	[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;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 20:

	==See Also==		==See Also==
-	*[[Ubiquitin ~~conjugating enzyme~~\|Ubiquitin ~~conjugating enzyme~~]]	+	*[[Ubiquitin protein ligase 3D structures\|Ubiquitin protein ligase 3D structures]]
-	*[[~~Ubiquitin protein ligase~~\|~~Ubiquitin protein ligase~~]]	+	*[[3D structures of ubiquitin conjugating enzyme\|3D structures of ubiquitin conjugating enzyme]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Ubiquitin--protein ligase]]~~	+	[[Category: Aitkenhead H]]
-	[[Category: Aitkenhead, H]]	+	[[Category: Anthony NG]]
-	[[Category: Anthony~~, N G~~]]	+	[[Category: Buetow L]]
-	[[Category: Buetow, L]]	+	[[Category: Dou H]]
-	[[Category: Dou, H]]	+	[[Category: Gabrielsen M]]
-	[[Category: Gabrielsen, M]]	+	[[Category: Huang DT]]
-	[[Category: Huang~~, D T~~]]	+	[[Category: Patel A]]
-	[[Category: Patel, A]]	+	[[Category: Sibbet GJ]]
-	[[Category: Sibbet~~, G J~~]]	+	[[Category: Smith BO]]
-	[[Category: Smith~~, B O]]~~	+
-	~~[[Category: E2]]~~	+
-	~~[[Category: Ligase]]~~	+
-	~~[[Category: Ring e3]]~~	+
-	~~[[Category: Ubiquitin~~]]	+

OCA at 08:10, 23 May 2019

OCA — Thu, 23 May 2019 08:10:37 GMT

←Older revision		Revision as of 08:10, 23 May 2019
Line 1:		Line 1:

	==RNF38-UbcH5B-UB complex==		==RNF38-UbcH5B-UB complex==
-	<StructureSection load='4v3k' size='340' side='right' caption='[[4v3k]], [[Resolution\|resolution]] 2.04Å' scene=''>	+	<StructureSection load='4v3k' size='340' side='right'caption='[[4v3k]], [[Resolution\|resolution]] 2.04Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4v3k]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V3K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V3K FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4v3k]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V3K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V3K FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4v3l\|4v3l]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4v3l\|4v3l]]</td></tr>
Line 20:		Line 20:
	</div>		</div>
	<div class="pdbe-citations 4v3k" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4v3k" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Ubiquitin conjugating enzyme\|Ubiquitin conjugating enzyme]]
		+	*[[Ubiquitin protein ligase\|Ubiquitin protein ligase]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Ubiquitin--protein ligase]]		[[Category: Ubiquitin--protein ligase]]
	[[Category: Aitkenhead, H]]		[[Category: Aitkenhead, H]]

OCA at 18:44, 1 February 2017

OCA — Wed, 01 Feb 2017 18:44:26 GMT

←Older revision		Revision as of 18:44, 1 February 2017
Line 1:		Line 1:
		+
	==RNF38-UbcH5B-UB complex==		==RNF38-UbcH5B-UB complex==
	<StructureSection load='4v3k' size='340' side='right' caption='[[4v3k]], [[Resolution\|resolution]] 2.04Å' scene=''>		<StructureSection load='4v3k' size='340' side='right' caption='[[4v3k]], [[Resolution\|resolution]] 2.04Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4v3l\|4v3l]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4v3l\|4v3l]]</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=4v3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v3k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4v3k RCSB], [http://www.ebi.ac.uk/pdbsum/4v3k 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=4v3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v3k OCA], [http://pdbe.org/4v3k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4v3k RCSB], [http://www.ebi.ac.uk/pdbsum/4v3k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4v3k ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	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 4v3k" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 11:01, 8 April 2015

OCA — Wed, 08 Apr 2015 11:01:15 GMT

←Older revision		Revision as of 11:01, 8 April 2015
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==RNF38-UbcH5B-UB complex==
		+	<StructureSection load='4v3k' size='340' side='right' caption='[[4v3k]], [[Resolution\|resolution]] 2.04Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4v3k]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V3K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V3K FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4v3l\|4v3l]]</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=4v3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v3k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4v3k RCSB], [http://www.ebi.ac.uk/pdbsum/4v3k PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://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> [[http://www.uniprot.org/uniprot/UBC_HUMAN UBC_HUMAN]] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.<ref>PMID:16543144</ref> <ref>PMID:19754430</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	RING ubiquitin ligases (E3) recruit ubiquitin-conjugate enzymes (E2) charged with ubiquitin (Ub) to catalyze ubiquitination. Non-covalent Ub binding to the backside of certain E2s promotes processive polyUb formation, but the mechanism remains elusive. Here, we show that backside bound Ub (UbB) enhances both RING-independent and RING-dependent UbcH5B-catalyzed donor Ub (UbD) transfer, but with a more prominent effect in RING-dependent transfer. UbB enhances RING E3s' affinities for UbcH5B-Ub, and RING E3-UbcH5B-Ub complex improves UbB's affinity for UbcH5B. A comparison of the crystal structures of a RING E3, RNF38, bound to UbcH5B-Ub in the absence and presence of UbB, together with molecular dynamics simulation and biochemical analyses, suggests UbB restricts the flexibility of UbcH5B's alpha1 and alpha1beta1 loop. UbB supports E3 function by stabilizing the RING E3-UbcH5B-Ub complex, thereby improving the catalytic efficiency of Ub transfer. Thus, UbB serves as an allosteric activator of RING E3-mediated Ub transfer.

-	~~The entry 4v3k is ON HOLD until Paper Publication~~	+	Activation of a Primed RING E3-E2-Ubiquitin Complex by Non-Covalent Ubiquitin.,Buetow L, Gabrielsen M, Anthony NG, Dou H, Patel A, Aitkenhead H, Sibbet GJ, Smith BO, Huang DT Mol Cell. 2015 Mar 18. pii: S1097-2765(15)00131-8. doi:, 10.1016/j.molcel.2015.02.017. PMID:25801170<ref>PMID:25801170</ref>

-	~~Authors: Buetow~~, L.~~, Gabrielsen, M~~.~~, Anthony, N.G., Dou, H., Patel, A., Aitkenhead, H., Sibbet, G.J., Smith, B.O., Huang, D.T~~.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description: RNF38-UbcH5B-UB complex~~	+	== References ==
-	[[Category: ~~Unreleased Structures~~]]	+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Ubiquitin--protein ligase]]
	[[Category: Aitkenhead, H]]		[[Category: Aitkenhead, H]]
		+	[[Category: Anthony, N G]]
	[[Category: Buetow, L]]		[[Category: Buetow, L]]
-	[[Category: Smith, B.O]]
-	[[Category: Anthony, N.G]]
	[[Category: Dou, H]]		[[Category: Dou, H]]
-	[[Category: Huang, D.T]]
	[[Category: Gabrielsen, M]]		[[Category: Gabrielsen, M]]
-	[[Category: ~~Sibbet~~, ~~G.J~~]]	+	[[Category: Huang, D T]]
	[[Category: Patel, A]]		[[Category: Patel, A]]
		+	[[Category: Sibbet, G J]]
		+	[[Category: Smith, B O]]
		+	[[Category: E2]]
		+	[[Category: Ligase]]
		+	[[Category: Ring e3]]
		+	[[Category: Ubiquitin]]

OCA at 10:49, 26 March 2015

OCA — Thu, 26 Mar 2015 10:49:56 GMT

←Older revision		Revision as of 10:49, 26 March 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4v3k is ON HOLD	+	The entry 4v3k is ON HOLD until Paper Publication

	Authors: Buetow, L., Gabrielsen, M., Anthony, N.G., Dou, H., Patel, A., Aitkenhead, H., Sibbet, G.J., Smith, B.O., Huang, D.T.		Authors: Buetow, L., Gabrielsen, M., Anthony, N.G., Dou, H., Patel, A., Aitkenhead, H., Sibbet, G.J., Smith, B.O., Huang, D.T.

-	Description: E3-E2-Ub	+	Description: RNF38-UbcH5B-UB complex
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
	[[Category: Aitkenhead, H]]		[[Category: Aitkenhead, H]]

OCA at 19:04, 24 December 2014

OCA — Wed, 24 Dec 2014 19:04:26 GMT

←Older revision		Revision as of 19:04, 24 December 2014
Line 6:		Line 6:

	Description: E3-E2-Ub		Description: E3-E2-Ub
		+	[[Category: Unreleased Structures]]
		+	[[Category: Aitkenhead, H]]
		+	[[Category: Buetow, L]]
		+	[[Category: Smith, B.O]]
		+	[[Category: Anthony, N.G]]
		+	[[Category: Dou, H]]
		+	[[Category: Huang, D.T]]
		+	[[Category: Gabrielsen, M]]
		+	[[Category: Sibbet, G.J]]
		+	[[Category: Patel, A]]

OCA: Protected "4v3k" [edit=sysop:move=sysop]

OCA — Wed, 29 Oct 2014 10:22:10 GMT

Protected "4v3k" [edit=sysop:move=sysop]

←Older revision

Revision as of 10:22, 29 October 2014

OCA: New page: '''Unreleased structure''' The entry 4v3k is ON HOLD Authors: Buetow, L., Gabrielsen, M., Anthony, N.G., Dou, H., Patel, A., Aitkenhead, H., Sibbet, G.J., Smith, B.O., Huang, D.T. Desc...

OCA — Wed, 29 Oct 2014 10:22:09 GMT

New page: '''Unreleased structure''' The entry 4v3k is ON HOLD Authors: Buetow, L., Gabrielsen, M., Anthony, N.G., Dou, H., Patel, A., Aitkenhead, H., Sibbet, G.J., Smith, B.O., Huang, D.T. Desc...

New page

'''Unreleased structure'''

The entry 4v3k is ON HOLD

Authors: Buetow, L., Gabrielsen, M., Anthony, N.G., Dou, H., Patel, A., Aitkenhead, H., Sibbet, G.J., Smith, B.O., Huang, D.T.

Description: E3-E2-Ub