4nrg - Revision history

OCA at 17:02, 20 September 2023

OCA — Wed, 20 Sep 2023 17:02:35 GMT

←Older revision		Revision as of 17:02, 20 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4nrg]] is a 2 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=4NRG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NRG FirstGlance]. <br>		<table><tr><td colspan='2'>[[4nrg]] is a 2 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=4NRG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NRG 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=4nrg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nrg OCA], [https://pdbe.org/4nrg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nrg RCSB], [https://www.ebi.ac.uk/pdbsum/4nrg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nrg 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]] 1.95Å</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=4nrg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nrg OCA], [https://pdbe.org/4nrg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nrg RCSB], [https://www.ebi.ac.uk/pdbsum/4nrg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nrg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 08:44, 11 January 2023

OCA — Wed, 11 Jan 2023 08:44:53 GMT

←Older revision		Revision as of 08:44, 11 January 2023
Line 3:		Line 3:
	<StructureSection load='4nrg' size='340' side='right'caption='[[4nrg]], [[Resolution\|resolution]] 1.95Å' scene=''>		<StructureSection load='4nrg' size='340' side='right'caption='[[4nrg]], [[Resolution\|resolution]] 1.95Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4nrg]] is a 2 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=4NRG OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4NRG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4nrg]] is a 2 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=4NRG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NRG FirstGlance]. <br>
-	</td></tr>~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4nr3\|4nr3]], [[4nri\|4nri]]</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=4nrg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nrg OCA], [https://pdbe.org/4nrg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nrg RCSB], [https://www.ebi.ac.uk/pdbsum/4nrg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nrg ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MMS2, UBE2V2, UEV2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), BLU, UBE2N ([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='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=4nrg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nrg OCA], [~~http~~://pdbe.org/4nrg PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4nrg RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4nrg PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4nrg ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/UB2V2_HUMAN UB2V2_HUMAN]] Has no ubiquitin ligase activity on its own. The UBE2V2/UBE2N heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'. This type of poly-ubiquitination 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.<ref>PMID:9705497</ref> <ref>PMID:10089880</ref> <ref>PMID:14562038</ref> <ref>PMID:20061386</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>	+	[https://www.uniprot.org/uniprot/UB2V2_HUMAN UB2V2_HUMAN] Has no ubiquitin ligase activity on its own. The UBE2V2/UBE2N heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'. This type of poly-ubiquitination 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.<ref>PMID:9705497</ref> <ref>PMID:10089880</ref> <ref>PMID:14562038</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 19:

	==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/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Ubiquitin--protein ligase]]~~	+	[[Category: Edwards RA]]
-	[[Category: Edwards~~, R A~~]]	+	[[Category: Glover JNM]]
-	[[Category: Glover~~, J N.M~~]]	+	[[Category: Hodge CD]]
-	[[Category: Hodge~~, C D]]~~	+
-	~~[[Category: E2]]~~	+
-	~~[[Category: Ligase]]~~	+
-	~~[[Category: Mms2]]~~	+
-	~~[[Category: Ubc13]]~~	+
-	~~[[Category: Ubiquitin conjugating enzyme~~]]	+

OCA at 08:56, 10 April 2019

OCA — Wed, 10 Apr 2019 08:56:48 GMT

←Older revision		Revision as of 08:56, 10 April 2019
Line 1:		Line 1:

	==Crystal Structure of a human Mms2/Ubc13 D118G mutant==		==Crystal Structure of a human Mms2/Ubc13 D118G mutant==
-	<StructureSection load='4nrg' size='340' side='right' caption='[[4nrg]], [[Resolution\|resolution]] 1.95Å' scene=''>	+	<StructureSection load='4nrg' size='340' side='right'caption='[[4nrg]], [[Resolution\|resolution]] 1.95Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4nrg]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NRG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NRG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4nrg]] is a 2 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=4NRG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NRG FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4nr3\|4nr3]], [[4nri\|4nri]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4nr3\|4nr3]], [[4nri\|4nri]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MMS2, UBE2V2, UEV2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), BLU, UBE2N ([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=4nrg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nrg OCA], [http://pdbe.org/4nrg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nrg RCSB], [http://www.ebi.ac.uk/pdbsum/4nrg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nrg 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=4nrg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nrg OCA], [http://pdbe.org/4nrg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nrg RCSB], [http://www.ebi.ac.uk/pdbsum/4nrg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nrg ProSAT]</span></td></tr>
Line 19:		Line 20:
	</div>		</div>
	<div class="pdbe-citations 4nrg" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4nrg" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Ubiquitin conjugating enzyme\|Ubiquitin conjugating enzyme]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Ubiquitin--protein ligase]]		[[Category: Ubiquitin--protein ligase]]
	[[Category: Edwards, R A]]		[[Category: Edwards, R A]]

OCA at 16:36, 4 August 2016

OCA — Thu, 04 Aug 2016 16:36:47 GMT

←Older revision		Revision as of 16:36, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal Structure of a human Mms2/Ubc13 D118G mutant==		==Crystal Structure of a human Mms2/Ubc13 D118G mutant==
	<StructureSection load='4nrg' size='340' side='right' caption='[[4nrg]], [[Resolution\|resolution]] 1.95Å' scene=''>		<StructureSection load='4nrg' size='340' side='right' caption='[[4nrg]], [[Resolution\|resolution]] 1.95Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4nr3\|4nr3]], [[4nri\|4nri]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4nr3\|4nr3]], [[4nri\|4nri]]</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=4nrg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nrg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nrg RCSB], [http://www.ebi.ac.uk/pdbsum/4nrg 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=4nrg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nrg OCA], [http://pdbe.org/4nrg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nrg RCSB], [http://www.ebi.ac.uk/pdbsum/4nrg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nrg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	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 4nrg" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 17:06, 24 December 2014

OCA — Wed, 24 Dec 2014 17:06:17 GMT

←Older revision		Revision as of 17:06, 24 December 2014
Line 7:		Line 7:
	<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=4nrg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nrg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nrg RCSB], [http://www.ebi.ac.uk/pdbsum/4nrg 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=4nrg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nrg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nrg RCSB], [http://www.ebi.ac.uk/pdbsum/4nrg PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/UB2V2_HUMAN UB2V2_HUMAN]] Has no ubiquitin ligase activity on its own. The UBE2V2/UBE2N heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'. This type of poly-ubiquitination 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.<ref>PMID:9705497</ref> <ref>PMID:10089880</ref> <ref>PMID:14562038</ref> <ref>PMID:20061386</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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 16:10, 10 December 2014

OCA — Wed, 10 Dec 2014 16:10:08 GMT

←Older revision		Revision as of 16:10, 10 December 2014
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Crystal Structure of a human Mms2/Ubc13 D118G mutant==
		+	<StructureSection load='4nrg' size='340' side='right' caption='[[4nrg]], [[Resolution\|resolution]] 1.95Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4nrg]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NRG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NRG FirstGlance]. <br>
		+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4nr3\|4nr3]], [[4nri\|4nri]]</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=4nrg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nrg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nrg RCSB], [http://www.ebi.ac.uk/pdbsum/4nrg PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Initiation of the DNA damage and innate immune responses is dependent upon the flow of chemical information through coupled protein-protein interaction networks and driven by the synthesis and recognition of Lys 63 linked polyubiquitin (polyUb) chains on adaptor proteins. The central chemical step in Lys 63-linked protein ubiquitination involves the reaction of a specific lysine on a target protein with Ub that is covalently attached as a thioester conjugate to the Ub conjugating enzyme (E2) Ubc13. The active site cysteine of Ubc13, and E2 enzymes in general, is buttressed by a flexible loop. The role of loop dynamics in catalysis was investigated by mutating the central and hinge residues to glycine. The loop dynamics were experimentally characterized through measurement of enzyme kinetics, main chain NMR relaxation, X-ray crystallographic studies, and in vivo studies in yeast. The experimental data were complemented by analysis of MD simulations of the dynamics and kinetics for the loop motion. The results show that fast pico- to nanosecond time scale active site loop fluctuations play a crucial role in regulating the catalytic activity of Ubc13 by functioning as a stochastic active site gate, which is characterized by precisely balanced rates of opening and closing. In vivo functional complementation assays in yeast demonstrate that defects within this regulatory mechanism can have profound biological consequences, given that Ubc13 is the only E2 dedicated to synthesizing Lys 63-linked polyUb chains.

-	~~The entry 4nrg is ON HOLD until Jan 16 2016~~	+	Stochastic Gate Dynamics Regulate the Catalytic Activity of Ubiquitination Enzymes.,Rout MK, Hodge CD, Markin CJ, Xu X, Glover JN, Xiao W, Spyracopoulos L J Am Chem Soc. 2014 Dec 5. PMID:25423605<ref>PMID:25423605</ref>

-	~~Authors: Hodge~~, C.D., Edwards, R.A., Glover, J.N.M.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description~~: ~~Crystal Structure of a human~~ Mms2/Ubc13 ~~D118G mutant~~	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Ubiquitin--protein ligase]]
		+	[[Category: Edwards, R A]]
		+	[[Category: Glover, J N.M]]
		+	[[Category: Hodge, C D]]
		+	[[Category: E2]]
		+	[[Category: Ligase]]
		+	[[Category: Mms2]]
		+	[[Category: Ubc13]]
		+	[[Category: Ubiquitin conjugating enzyme]]

OCA at 07:23, 5 November 2014

OCA — Wed, 05 Nov 2014 07:23:18 GMT

←Older revision		Revision as of 07:23, 5 November 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4nrg is ON HOLD until ~~Paper Publication~~	+	The entry 4nrg is ON HOLD until Jan 16 2016

	Authors: Hodge, C.D., Edwards, R.A., Glover, J.N.M.		Authors: Hodge, C.D., Edwards, R.A., Glover, J.N.M.

	Description: Crystal Structure of a human Mms2/Ubc13 D118G mutant		Description: Crystal Structure of a human Mms2/Ubc13 D118G mutant

OCA at 10:19, 5 February 2014

OCA — Wed, 05 Feb 2014 10:19:40 GMT

←Older revision		Revision as of 10:19, 5 February 2014
Line 3:		Line 3:
	The entry 4nrg is ON HOLD until Paper Publication		The entry 4nrg is ON HOLD until Paper Publication

-	Authors: Hodge, C.D., Edwards, R.A.	+	Authors: Hodge, C.D., Edwards, R.A., Glover, J.N.M.

	Description: Crystal Structure of a human Mms2/Ubc13 D118G mutant		Description: Crystal Structure of a human Mms2/Ubc13 D118G mutant

OCA at 09:20, 18 December 2013

OCA — Wed, 18 Dec 2013 09:20:41 GMT

←Older revision		Revision as of 09:20, 18 December 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Hodge, C.D., Edwards, R.A.		Authors: Hodge, C.D., Edwards, R.A.

	Description: Crystal Structure of a human Mms2/Ubc13 D118G mutant		Description: Crystal Structure of a human Mms2/Ubc13 D118G mutant

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

OCA — Wed, 04 Dec 2013 06:53:39 GMT

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

←Older revision

Revision as of 06:53, 4 December 2013