6cgh - Revision history

OCA at 10:39, 14 June 2023

OCA — Wed, 14 Jun 2023 10:39:51 GMT

←Older revision		Revision as of 10:39, 14 June 2023
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	==Solution structure of the four-helix bundle region of human J-protein Zuotin, a component of ribosome-associated complex (RAC)==		==Solution structure of the four-helix bundle region of human J-protein Zuotin, a component of ribosome-associated complex (RAC)==
-	<StructureSection load='6cgh' size='340' side='right'caption='[[6cgh~~]], [[NMR_Ensembles_of_Models \| 20 NMR models~~]]' scene=''>	+	<StructureSection load='6cgh' size='340' side='right'caption='[[6cgh]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6cgh]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CGH OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6CGH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6cgh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CGH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CGH FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">DNAJC2, MPHOSPH11, MPP11, ZRF1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6cgh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cgh OCA], [https://pdbe.org/6cgh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cgh RCSB], [https://www.ebi.ac.uk/pdbsum/6cgh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cgh 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=6cgh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cgh OCA], [~~http~~://pdbe.org/6cgh PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6cgh RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6cgh PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6cgh ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/DNJC2_HUMAN DNJC2_HUMAN]] Acts both as a chaperone in the cytosol and as a chromatin regulator in the nucleus. When cytosolic, acts as a molecular chaperone: component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones HSPA14 that bind to the nascent polypeptide chain. When nuclear, mediates the switching from polycomb-repressed genes to an active state: specifically recruited at histone H2A ubiquitinated at 'Lys-119' (H2AK119ub), and promotes the displacement of the polycomb PRC1 complex from chromatin, thereby facilitating transcription activation. Specifically binds DNA sequence 5'-GTCAAGC-3'.<ref>PMID:16002468</ref> <ref>PMID:15802566</ref> <ref>PMID:21179169</ref>	+	[https://www.uniprot.org/uniprot/DNJC2_HUMAN DNJC2_HUMAN] Acts both as a chaperone in the cytosol and as a chromatin regulator in the nucleus. When cytosolic, acts as a molecular chaperone: component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones HSPA14 that bind to the nascent polypeptide chain. When nuclear, mediates the switching from polycomb-repressed genes to an active state: specifically recruited at histone H2A ubiquitinated at 'Lys-119' (H2AK119ub), and promotes the displacement of the polycomb PRC1 complex from chromatin, thereby facilitating transcription activation. Specifically binds DNA sequence 5'-GTCAAGC-3'.<ref>PMID:16002468</ref> <ref>PMID:15802566</ref> <ref>PMID:21179169</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==
	*[[DnaJ homolog 3D structures\|DnaJ homolog 3D structures]]		*[[DnaJ homolog 3D structures\|DnaJ homolog 3D structures]]
		+	*[[Heat Shock Protein structures\|Heat Shock Protein structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Ciesielski~~, S J~~]]	+	[[Category: Ciesielski SJ]]
-	[[Category: Cornilescu, G]]	+	[[Category: Cornilescu G]]
-	[[Category: Craig~~, E A~~]]	+	[[Category: Craig EA]]
-	[[Category: Lee, W]]	+	[[Category: Lee W]]
-	[[Category: Markley~~, J L~~]]	+	[[Category: Markley JL]]
-	[[Category: Shrestha~~, O K~~]]	+	[[Category: Shrestha OK]]
-	[[Category: Tonelli, M]]	+	[[Category: Tonelli M]]
-	~~[[Category: Chaperone]]~~	+
-	~~[[Category: Dnajc2]]~~	+
-	~~[[Category: Hsp40]]~~	+
-	~~[[Category: Hsp70]]~~	+
-	~~[[Category: J-protein]]~~	+
-	~~[[Category: Molecular chaperone]]~~	+
-	~~[[Category: Mpp11]]~~	+
-	~~[[Category: Zuotin~~]]	+

OCA at 09:40, 18 December 2019

OCA — Wed, 18 Dec 2019 09:40:21 GMT

←Older revision		Revision as of 09:40, 18 December 2019
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	<StructureSection load='6cgh' size='340' side='right'caption='[[6cgh]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='6cgh' size='340' side='right'caption='[[6cgh]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6cgh]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CGH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CGH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6cgh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CGH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CGH FirstGlance]. <br>
-	</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=6cgh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cgh OCA], [http://pdbe.org/6cgh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cgh RCSB], [http://www.ebi.ac.uk/pdbsum/6cgh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cgh ProSAT]</span></td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">DNAJC2, MPHOSPH11, MPP11, ZRF1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6cgh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cgh OCA], [http://pdbe.org/6cgh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cgh RCSB], [http://www.ebi.ac.uk/pdbsum/6cgh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cgh ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 6cgh" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 6cgh" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[DnaJ homolog 3D structures\|DnaJ homolog 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Ciesielski, S J]]		[[Category: Ciesielski, S J]]

OCA at 05:29, 12 June 2019

OCA — Wed, 12 Jun 2019 05:29:23 GMT

←Older revision		Revision as of 05:29, 12 June 2019
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6cgh is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==Solution structure of the four-helix bundle region of human J-protein Zuotin, a component of ribosome-associated complex (RAC)==
		+	<StructureSection load='6cgh' size='340' side='right'caption='[[6cgh]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[6cgh]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CGH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CGH FirstGlance]. <br>
		+	</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=6cgh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cgh OCA], [http://pdbe.org/6cgh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cgh RCSB], [http://www.ebi.ac.uk/pdbsum/6cgh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cgh ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/DNJC2_HUMAN DNJC2_HUMAN]] Acts both as a chaperone in the cytosol and as a chromatin regulator in the nucleus. When cytosolic, acts as a molecular chaperone: component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones HSPA14 that bind to the nascent polypeptide chain. When nuclear, mediates the switching from polycomb-repressed genes to an active state: specifically recruited at histone H2A ubiquitinated at 'Lys-119' (H2AK119ub), and promotes the displacement of the polycomb PRC1 complex from chromatin, thereby facilitating transcription activation. Specifically binds DNA sequence 5'-GTCAAGC-3'.<ref>PMID:16002468</ref> <ref>PMID:15802566</ref> <ref>PMID:21179169</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The J-domain protein Zuotin is a multi-domain eukaryotic Hsp70 co-chaperone. Though it is primarily ribosome-associated, positioned at the exit of the 60S subunit tunnel where it promotes folding of nascent polypeptide chains, Zuotin also has off-ribosome functions. Domains of Zuotin needed for 60S association and interaction with Hsp70 are conserved in eukaryotes. However, whether the 4-helix bundle (4HB) domain is conserved remains an open question. We undertook evolutionary and structural approaches to clarify this issue. We found that the 4HB segment of human Zuotin also forms a bundle of 4 helices. The positive charge of Helix I, which in Saccharomyces cerevisiae is responsible for interaction with the 40S subunit, is particularly conserved. However, the C-termini of fungal and human 4HBs are not similar. In fungi the C-terminal segment forms a plug that folds back into the bundle; in S. cerevisiae it plays an important role in bundle stability and, off the ribosome, in transcriptional activation. In human, C-terminal helix IV of the 4HB is extended, protruding from the bundle. This extension serves as a linker to the regulatory SANT domains, which are present in animals, plants and protists, but not fungi. Further analysis of Zuotin sequences revealed that the plug likely arose as a result of genomic rearrangement upon SANT domain loss early in the fungal lineage. In the lineage leading to S. cerevisiae, the 4HB was subjected to positive selection with the plug becoming increasingly hydrophobic. Eventually, these hydrophobic plug residues were coopted for a novel regulatory function-activation of a recently emerged transcription factor, Pdr1. Our data suggests that Zuotin evolved off-ribosome functions twice-once involving SANT domains, then later in fungi, after SANT domain loss, by coopting the hydrophobic plug. Zuotin serves as an example of complex intertwining of molecular chaperone function and cell regulation.

-	~~Authors~~:	+	Structure and evolution of the 4-helix bundle domain of Zuotin, a J-domain protein co-chaperone of Hsp70.,Shrestha OK, Sharma R, Tomiczek B, Lee W, Tonelli M, Cornilescu G, Stolarska M, Nierzwicki L, Czub J, Markley JL, Marszalek J, Ciesielski SJ, Craig EA PLoS One. 2019 May 15;14(5):e0217098. doi: 10.1371/journal.pone.0217098., eCollection 2019. PMID:31091298<ref>PMID:31091298</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
		+	<div class="pdbe-citations 6cgh" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Ciesielski, S J]]
		+	[[Category: Cornilescu, G]]
		+	[[Category: Craig, E A]]
		+	[[Category: Lee, W]]
		+	[[Category: Markley, J L]]
		+	[[Category: Shrestha, O K]]
		+	[[Category: Tonelli, M]]
		+	[[Category: Chaperone]]
		+	[[Category: Dnajc2]]
		+	[[Category: Hsp40]]
		+	[[Category: Hsp70]]
		+	[[Category: J-protein]]
		+	[[Category: Molecular chaperone]]
		+	[[Category: Mpp11]]
		+	[[Category: Zuotin]]

OCA at 12:24, 11 April 2018

OCA — Wed, 11 Apr 2018 12:24:23 GMT

←Older revision		Revision as of 12:24, 11 April 2018
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6cgh is ON HOLD	+	The entry 6cgh is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "6cgh" [edit=sysop:move=sysop]

OCA — Wed, 28 Feb 2018 05:03:32 GMT

Protected "6cgh" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:03, 28 February 2018

OCA: New page: '''Unreleased structure''' The entry 6cgh is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Wed, 28 Feb 2018 05:03:30 GMT

New page: '''Unreleased structure''' The entry 6cgh is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 6cgh is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]