5cw3 - Revision history

OCA at 12:21, 6 March 2024

2024-03-06T12:21:50Z

←Older revision		Revision as of 12:21, 6 March 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5cw3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Camponotus_floridanus Camponotus floridanus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CW3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CW3 FirstGlance]. <br>		<table><tr><td colspan='2'>[[5cw3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Camponotus_floridanus Camponotus floridanus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CW3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CW3 FirstGlance]. <br>
-	</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>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.55Å</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5cw3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cw3 OCA], [https://pdbe.org/5cw3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cw3 RCSB], [https://www.ebi.ac.uk/pdbsum/5cw3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cw3 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=5cw3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cw3 OCA], [https://pdbe.org/5cw3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cw3 RCSB], [https://www.ebi.ac.uk/pdbsum/5cw3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cw3 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/BRCC3_CAMFO BRCC3_CAMFO] Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains, leaving the last ubiquitin chain attached to its substrates. Catalytic subunit of the BRISC complex; does not have activity by itself, but needs to be associated into a heterotetramer with ABRAXAS2 for minimal in vitro activity (PubMed:26344097). Plays a role in regulating the onset of apoptosis via its role in modulating 'Lys-63'-linked ubiquitination of target proteins (By similarity). Required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating spindle assembly factors (By similarity).[UniProtKB:Q15018][UniProtKB:Q3TCJ1]<ref>PMID:26344097</ref>		[https://www.uniprot.org/uniprot/BRCC3_CAMFO BRCC3_CAMFO] Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains, leaving the last ubiquitin chain attached to its substrates. Catalytic subunit of the BRISC complex; does not have activity by itself, but needs to be associated into a heterotetramer with ABRAXAS2 for minimal in vitro activity (PubMed:26344097). Plays a role in regulating the onset of apoptosis via its role in modulating 'Lys-63'-linked ubiquitination of target proteins (By similarity). Required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating spindle assembly factors (By similarity).[UniProtKB:Q15018][UniProtKB:Q3TCJ1]<ref>PMID:26344097</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	BRCC36 is a Zn(2+)-dependent deubiquitinating enzyme (DUB) that hydrolyzes lysine-63-linked ubiquitin chains as part of distinct macromolecular complexes that participate in either interferon signaling or DNA-damage recognition. The MPN(+) domain protein BRCC36 associates with pseudo DUB MPN(-) proteins KIAA0157 or Abraxas, which are essential for BRCC36 enzymatic activity. To understand the basis for BRCC36 regulation, we have solved the structure of an active BRCC36-KIAA0157 heterodimer and an inactive BRCC36 homodimer. Structural and functional characterizations show how BRCC36 is switched to an active conformation by contacts with KIAA0157. Higher-order association of BRCC36 and KIAA0157 into a dimer of heterodimers (super dimers) was required for DUB activity and interaction with targeting proteins SHMT2 and RAP80. These data provide an explanation of how an inactive pseudo DUB allosterically activates a cognate DUB partner and implicates super dimerization as a new regulatory mechanism underlying BRCC36 DUB activity, subcellular localization, and biological function.
-
-	Higher-Order Assembly of BRCC36-KIAA0157 Is Required for DUB Activity and Biological Function.,Zeqiraj E, Tian L, Piggott CA, Pillon MC, Duffy NM, Ceccarelli DF, Keszei AF, Lorenzen K, Kurinov I, Orlicky S, Gish GD, Heck AJ, Guarne A, Greenberg RA, Sicheri F Mol Cell. 2015 Sep 17;59(6):970-83. doi: 10.1016/j.molcel.2015.07.028. Epub 2015 , Sep 3. PMID:26344097<ref>PMID:26344097</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 5cw3" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:10, 21 June 2023

2023-06-21T10:10:28Z

←Older revision		Revision as of 10:10, 21 June 2023
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	==Structure of CfBRCC36-CfKIAA0157 complex (Zn Edge)==		==Structure of CfBRCC36-CfKIAA0157 complex (Zn Edge)==
-	<StructureSection load='5cw3' size='340' side='right' caption='[[5cw3]], [[Resolution\|resolution]] 2.55Å' scene=''>	+	<StructureSection load='5cw3' size='340' side='right'caption='[[5cw3]], [[Resolution\|resolution]] 2.55Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5cw3]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Camfo Camfo~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CW3 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5CW3 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5cw3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Camponotus_floridanus Camponotus floridanus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CW3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CW3 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" id="ligandDat"><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">[[5cw6\|5cw6]], [[5cw5\|5cw5]], [[5cw4\|5cw4]]</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=5cw3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cw3 OCA], [https://pdbe.org/5cw3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cw3 RCSB], [https://www.ebi.ac.uk/pdbsum/5cw3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cw3 ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">EAG_15736 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=104421 CAMFO]), EAG_01033 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=104421 CAMFO])</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=5cw3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cw3 OCA], [~~http~~://pdbe.org/5cw3 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5cw3 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5cw3 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5cw3 ProSAT]</span></td></tr>	+
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/BRCC3_CAMFO BRCC3_CAMFO] Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains, leaving the last ubiquitin chain attached to its substrates. Catalytic subunit of the BRISC complex; does not have activity by itself, but needs to be associated into a heterotetramer with ABRAXAS2 for minimal in vitro activity (PubMed:26344097). Plays a role in regulating the onset of apoptosis via its role in modulating 'Lys-63'-linked ubiquitination of target proteins (By similarity). Required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating spindle assembly factors (By similarity).[UniProtKB:Q15018][UniProtKB:Q3TCJ1]<ref>PMID:26344097</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Camfo~~]]	+	[[Category: Camponotus floridanus]]
-	[[Category: ~~Zeqiraj, E~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Metal binding protein]]~~	+	[[Category: Zeqiraj E]]
-	~~[[Category: Metal dependent enzyme~~]]	+

OCA at 17:17, 16 November 2017

2017-11-16T17:17:04Z

←Older revision		Revision as of 17:17, 16 November 2017
Line 1:		Line 1:
		+
	==Structure of CfBRCC36-CfKIAA0157 complex (Zn Edge)==		==Structure of CfBRCC36-CfKIAA0157 complex (Zn Edge)==
	<StructureSection load='5cw3' size='340' side='right' caption='[[5cw3]], [[Resolution\|resolution]] 2.55Å' scene=''>		<StructureSection load='5cw3' size='340' side='right' caption='[[5cw3]], [[Resolution\|resolution]] 2.55Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5cw3]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CW3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CW3 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5cw3]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Camfo Camfo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CW3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CW3 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='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5cw6\|5cw6]], [[5cw5\|5cw5]], [[5cw4\|5cw4]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5cw6\|5cw6]], [[5cw5\|5cw5]], [[5cw4\|5cw4]]</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=5cw3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cw3 OCA], [http://pdbe.org/5cw3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cw3 RCSB], [http://www.ebi.ac.uk/pdbsum/5cw3 PDBsum]</span></td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">EAG_15736 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=104421 CAMFO]), EAG_01033 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=104421 CAMFO])</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=5cw3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cw3 OCA], [http://pdbe.org/5cw3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cw3 RCSB], [http://www.ebi.ac.uk/pdbsum/5cw3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cw3 ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 20:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Camfo]]
	[[Category: Zeqiraj, E]]		[[Category: Zeqiraj, E]]
	[[Category: Metal binding protein]]		[[Category: Metal binding protein]]
	[[Category: Metal dependent enzyme]]		[[Category: Metal dependent enzyme]]

OCA at 07:48, 30 September 2015

2015-09-30T07:48:52Z

←Older revision		Revision as of 07:48, 30 September 2015
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Structure of CfBRCC36-CfKIAA0157 complex (Zn Edge)==
		+	<StructureSection load='5cw3' size='340' side='right' caption='[[5cw3]], [[Resolution\|resolution]] 2.55Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5cw3]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CW3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CW3 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='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5cw6\|5cw6]], [[5cw5\|5cw5]], [[5cw4\|5cw4]]</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=5cw3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cw3 OCA], [http://pdbe.org/5cw3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cw3 RCSB], [http://www.ebi.ac.uk/pdbsum/5cw3 PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	BRCC36 is a Zn(2+)-dependent deubiquitinating enzyme (DUB) that hydrolyzes lysine-63-linked ubiquitin chains as part of distinct macromolecular complexes that participate in either interferon signaling or DNA-damage recognition. The MPN(+) domain protein BRCC36 associates with pseudo DUB MPN(-) proteins KIAA0157 or Abraxas, which are essential for BRCC36 enzymatic activity. To understand the basis for BRCC36 regulation, we have solved the structure of an active BRCC36-KIAA0157 heterodimer and an inactive BRCC36 homodimer. Structural and functional characterizations show how BRCC36 is switched to an active conformation by contacts with KIAA0157. Higher-order association of BRCC36 and KIAA0157 into a dimer of heterodimers (super dimers) was required for DUB activity and interaction with targeting proteins SHMT2 and RAP80. These data provide an explanation of how an inactive pseudo DUB allosterically activates a cognate DUB partner and implicates super dimerization as a new regulatory mechanism underlying BRCC36 DUB activity, subcellular localization, and biological function.

-	~~The entry 5cw3 is ON HOLD until Paper Publication~~	+	Higher-Order Assembly of BRCC36-KIAA0157 Is Required for DUB Activity and Biological Function.,Zeqiraj E, Tian L, Piggott CA, Pillon MC, Duffy NM, Ceccarelli DF, Keszei AF, Lorenzen K, Kurinov I, Orlicky S, Gish GD, Heck AJ, Guarne A, Greenberg RA, Sicheri F Mol Cell. 2015 Sep 17;59(6):970-83. doi: 10.1016/j.molcel.2015.07.028. Epub 2015 , Sep 3. PMID:26344097<ref>PMID:26344097</ref>

-	~~Authors: Zeqiraj~~, E.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description: Structure of CfBRCC36~~-~~CfKIAA0157 complex (Zn Edge)~~	+	<div class="pdbe-citations 5cw3" style="background-color:#fffaf0;"></div>
-	~~[[Category~~: ~~Unreleased Structures]]~~	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Zeqiraj, E]]		[[Category: Zeqiraj, E]]
		+	[[Category: Metal binding protein]]
		+	[[Category: Metal dependent enzyme]]

OCA at 10:59, 2 September 2015

2015-09-02T10:59:43Z

←Older revision		Revision as of 10:59, 2 September 2015
Line 5:		Line 5:
	Authors: Zeqiraj, E.		Authors: Zeqiraj, E.

-	Description: Structure of ~~a metal dependent enzyme CFBRCC36~~	+	Description: Structure of CfBRCC36-CfKIAA0157 complex (Zn Edge)
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
	[[Category: Zeqiraj, E]]		[[Category: Zeqiraj, E]]

OCA at 12:11, 26 August 2015

2015-08-26T12:11:35Z

←Older revision		Revision as of 12:11, 26 August 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5cw3 is ON HOLD	+	The entry 5cw3 is ON HOLD until Paper Publication

	Authors: Zeqiraj, E.		Authors: Zeqiraj, E.

OCA: Protected "5cw3" [edit=sysop:move=sysop]

2015-08-05T19:02:45Z

Protected "5cw3" [edit=sysop:move=sysop]

←Older revision

Revision as of 19:02, 5 August 2015

OCA: New page: '''Unreleased structure''' The entry 5cw3 is ON HOLD Authors: Zeqiraj, E. Description: Structure of a metal dependent enzyme CFBRCC36 Category: Unreleased Structures [[Category: Ze...

2015-08-05T19:02:43Z

New page: '''Unreleased structure''' The entry 5cw3 is ON HOLD Authors: Zeqiraj, E. Description: Structure of a metal dependent enzyme CFBRCC36 Category: Unreleased Structures [[Category: Ze...

New page

'''Unreleased structure'''

The entry 5cw3 is ON HOLD

Authors: Zeqiraj, E.

Description: Structure of a metal dependent enzyme CFBRCC36
[[Category: Unreleased Structures]]
[[Category: Zeqiraj, E]]