5tte - Revision history

OCA at 13:11, 4 October 2023

OCA — Wed, 04 Oct 2023 13:11:45 GMT

←Older revision		Revision as of 13:11, 4 October 2023
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	<StructureSection load='5tte' size='340' side='right'caption='[[5tte]], [[Resolution\|resolution]] 3.50Å' scene=''>		<StructureSection load='5tte' size='340' side='right'caption='[[5tte]], [[Resolution\|resolution]] 3.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5tte]] is a 3 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Canadian_hard_winter_wheat Canadian hard winter wheat~~] and [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TTE OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5TTE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5tte]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Triticum_aestivum Triticum aestivum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TTE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TTE FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><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]] 3.501Å</td></tr>
-	~~<tr~~ id~~='gene'><td class~~="~~sblockLbl~~">~~<b>~~[[~~Gene~~\|~~Gene:~~]]~~</b></td><td class="sblockDat">ARIH1, ARI, MOP6, UBCH7BP, HUSSY-27 ([http://www~~.~~ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info~~&~~srchmode=5&id=9606 HUMAN]), UBE2L3, UBCE7, UBCH7 ([http://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=ZN:ZINC+ION'>ZN</scene></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=5tte FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tte OCA], [https://pdbe.org/5tte PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tte RCSB], [https://www.ebi.ac.uk/pdbsum/5tte PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tte ProSAT]</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=5tte FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tte OCA], [~~http~~://pdbe.org/5tte PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5tte RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5tte PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5tte ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/ARI1_HUMAN ARI1_HUMAN]] E3 ubiquitin-protein ligase, which catalyzes polyubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 UBE2L3. May play a role in protein translation by mediating polyubiquitination of EIF4E2, leading to its subsequent degradation.<ref>PMID:14623119</ref> <ref>PMID:21532592</ref> <ref>PMID:15236971</ref> [[http://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/ARI1_HUMAN ARI1_HUMAN] E3 ubiquitin-protein ligase, which catalyzes polyubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 UBE2L3. May play a role in protein translation by mediating polyubiquitination of EIF4E2, leading to its subsequent degradation.<ref>PMID:14623119</ref> <ref>PMID:21532592</ref> <ref>PMID:15236971</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	==See Also==		==See Also==
-	*[[Ubiquitin\|Ubiquitin]]	+	*[[Ubiquitin protein ligase 3D structures\|Ubiquitin protein ligase 3D structures]]
-	*[[~~Ubiquitin conjugating enzyme~~\|~~Ubiquitin conjugating enzyme~~]]	+	*[[3D structures of ubiquitin\|3D structures of ubiquitin]]
-	*[[~~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: ~~Canadian hard winter wheat]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: E2 ubiquitin-conjugating enzyme]]~~	+
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Lv, Z~~]]	+	[[Category: Triticum aestivum]]
-	[[Category: ~~Olsen, S K~~]]	+	[[Category: Lv Z]]
-	[[Category: ~~Yuan, L~~]]	+	[[Category: Olsen SK]]
-	[[Category: ~~Complex]]~~	+	[[Category: Yuan L]]
-	~~[[Category: E2]]~~	+
-	~~[[Category: Ligase]]~~	+
-	~~[[Category: Rbr e3 ubiquitin ligase]]~~	+
-	~~[[Category: Transferase]]~~	+
-	~~[[Category: Transthioloation~~]]	+

OCA at 09:05, 1 January 2020

OCA — Wed, 01 Jan 2020 09:05:50 GMT

←Older revision		Revision as of 09:05, 1 January 2020
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	==Crystal Structure of an RBR E3 ubiquitin ligase in complex with an E2-Ub thioester intermediate mimic==		==Crystal Structure of an RBR E3 ubiquitin ligase in complex with an E2-Ub thioester intermediate mimic==
-	<StructureSection load='5tte' size='340' side='right' caption='[[5tte]], [[Resolution\|resolution]] 3.50Å' scene=''>	+	<StructureSection load='5tte' size='340' side='right'caption='[[5tte]], [[Resolution\|resolution]] 3.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5tte]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TTE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TTE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5tte]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Canadian_hard_winter_wheat Canadian hard winter wheat] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TTE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TTE FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><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=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ARIH1, ARI, MOP6, UBCH7BP, HUSSY-27 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), UBE2L3, UBCE7, UBCH7 ([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/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='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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5tte FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tte OCA], [http://pdbe.org/5tte PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tte RCSB], [http://www.ebi.ac.uk/pdbsum/5tte PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tte ProSAT]</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=5tte FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tte OCA], [http://pdbe.org/5tte PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tte RCSB], [http://www.ebi.ac.uk/pdbsum/5tte PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tte ProSAT]</span></td></tr>
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	</div>		</div>
	<div class="pdbe-citations 5tte" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5tte" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Ubiquitin\|Ubiquitin]]
		+	*[[Ubiquitin conjugating enzyme\|Ubiquitin conjugating enzyme]]
		+	*[[Ubiquitin protein ligase\|Ubiquitin protein ligase]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Canadian hard winter wheat]]
	[[Category: E2 ubiquitin-conjugating enzyme]]		[[Category: E2 ubiquitin-conjugating enzyme]]
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Lv, Z]]		[[Category: Lv, Z]]
	[[Category: Olsen, S K]]		[[Category: Olsen, S K]]

OCA at 07:00, 25 October 2017

OCA — Wed, 25 Oct 2017 07:00:22 GMT

←Older revision		Revision as of 07:00, 25 October 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5tte is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==Crystal Structure of an RBR E3 ubiquitin ligase in complex with an E2-Ub thioester intermediate mimic==
		+	<StructureSection load='5tte' size='340' side='right' caption='[[5tte]], [[Resolution\|resolution]] 3.50Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5tte]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TTE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TTE FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5tte FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tte OCA], [http://pdbe.org/5tte PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tte RCSB], [http://www.ebi.ac.uk/pdbsum/5tte PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tte ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ARI1_HUMAN ARI1_HUMAN]] E3 ubiquitin-protein ligase, which catalyzes polyubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 UBE2L3. May play a role in protein translation by mediating polyubiquitination of EIF4E2, leading to its subsequent degradation.<ref>PMID:14623119</ref> <ref>PMID:21532592</ref> <ref>PMID:15236971</ref> [[http://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>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	RING-in-between-RING (RBR) ubiquitin (Ub) E3 ligases function with Ub E2s through a RING/HECT hybrid mechanism to conjugate Ub to target proteins. Here, we report the crystal structure of the RBR E3, HHARI, in complex with a UbcH7 ~ Ub thioester mimetic which reveals the molecular basis for the specificity of this cognate E2/RBR E3 pair. The structure also reveals mechanistically important conformational changes in the RING1 and UBA-like domains of HHARI that accompany UbcH7 ~ Ub binding and provides a molecular basis by which HHARI recruits E2 ~ Ub in an 'open' conformation. In addition to optimally functioning with an E2 that solely performs transthiolation, our data suggests that HHARI prevents spurious discharge of Ub from E2 to lysine residues by: (1) harboring structural elements that block E2 ~ Ub from adopting a 'closed' conformation and (2) participating in contacts to ubiquitin that promote an open E2 ~ Ub conformation.HHARI is a RING-in-between-RING (RBR) ubiquitin (Ub) E3 ligase. Here the authors present the crystal structure of HHARI with the UbcH7 ~ Ub thioester intermediate mimetic, which reveals that HHARI binds this E2 ~ Ub in an open conformation and explains the specificity of this cognate RBR E3/E2 pair.

-	~~Authors~~:	+	Structural insights into the mechanism and E2 specificity of the RBR E3 ubiquitin ligase HHARI.,Yuan L, Lv Z, Atkison JH, Olsen SK Nat Commun. 2017 Aug 8;8(1):211. doi: 10.1038/s41467-017-00272-6. PMID:28790309<ref>PMID:28790309</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
		+	<div class="pdbe-citations 5tte" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: E2 ubiquitin-conjugating enzyme]]
		+	[[Category: Lv, Z]]
		+	[[Category: Olsen, S K]]
		+	[[Category: Yuan, L]]
		+	[[Category: Complex]]
		+	[[Category: E2]]
		+	[[Category: Ligase]]
		+	[[Category: Rbr e3 ubiquitin ligase]]
		+	[[Category: Transferase]]
		+	[[Category: Transthioloation]]

OCA at 14:46, 2 January 2017

OCA — Mon, 02 Jan 2017 14:46:01 GMT

←Older revision		Revision as of 14:46, 2 January 2017
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5tte is ON HOLD	+	The entry 5tte is ON HOLD until Paper Publication

	Authors:		Authors:

OCA at 20:04, 22 December 2016

OCA — Thu, 22 Dec 2016 20:04:20 GMT

←Older revision		Revision as of 20:04, 22 December 2016
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5tte is ON HOLD ~~until Paper Publication~~	+	The entry 5tte is ON HOLD

	Authors:		Authors:

OCA: Protected "5tte" [edit=sysop:move=sysop]

OCA — Fri, 09 Dec 2016 17:51:14 GMT

Protected "5tte" [edit=sysop:move=sysop]

←Older revision

Revision as of 17:51, 9 December 2016

OCA: New page: '''Unreleased structure''' The entry 5tte is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures

OCA — Fri, 09 Dec 2016 17:51:13 GMT

New page: '''Unreleased structure''' The entry 5tte is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 5tte is ON HOLD until Paper Publication

Authors:

Description:
[[Category: Unreleased Structures]]