6ks7 - Revision history

OCA at 10:44, 27 March 2024

OCA — Wed, 27 Mar 2024 10:44:05 GMT

←Older revision		Revision as of 10:44, 27 March 2024
Line 3:		Line 3:
	<SX load='6ks7' size='340' side='right' viewer='molstar' caption='[[6ks7]], [[Resolution\|resolution]] 4.62Å' scene=''>		<SX load='6ks7' size='340' side='right' viewer='molstar' caption='[[6ks7]], [[Resolution\|resolution]] 4.62Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6ks7]] is a 16 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Saccharomyces_cerevisiae_s288c~~ Saccharomyces cerevisiae ~~s288c~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KS7 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=6KS7 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6ks7]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KS7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KS7 FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=6ks7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ks7 OCA], [~~http~~://pdbe.org/6ks7 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6ks7 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6ks7 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6ks7 ProSAT]</span></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution\|Resolution]] 4.62Å</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=6ks7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ks7 OCA], [https://pdbe.org/6ks7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ks7 RCSB], [https://www.ebi.ac.uk/pdbsum/6ks7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ks7 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[http://www.uniprot.org/uniprot/TCPE_YEAST TCPE_YEAST]] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation. [[http://www.uniprot.org/uniprot/TCPB_YEAST TCPB_YEAST]] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation. [[http://www.uniprot.org/uniprot/TCPG_YEAST TCPG_YEAST]] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation. [[http://www.uniprot.org/uniprot/TCPZ_YEAST TCPZ_YEAST]] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation. [[http://www.uniprot.org/uniprot/TCPA_YEAST TCPA_YEAST]] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation. [[http://www.uniprot.org/uniprot/TCPQ_YEAST TCPQ_YEAST]] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation (By similarity). [[http://www.uniprot.org/uniprot/TCPH_YEAST TCPH_YEAST]] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation (By similarity). [[http://www.uniprot.org/uniprot/TCPD_YEAST TCPD_YEAST]] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation.	+	[https://www.uniprot.org/uniprot/TCPH_YEAST TCPH_YEAST] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation (By similarity).
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	TRiC/CCT assists the folding of approximately 10% of cytosolic proteins through an ATP-driven conformational cycle and is essential in maintaining protein homeostasis. Here, we determined an ensemble of cryo-electron microscopy (cryo-EM) structures of yeast TRiC at various nucleotide concentrations, with 4 open-state maps resolved at near-atomic resolutions, and a closed-state map at atomic resolution, revealing an extra layer of an unforeseen N-terminal allosteric network. We found that, during TRiC ring closure, the CCT7 subunit moves first, responding to nucleotide binding; CCT4 is the last to bind ATP, serving as an ATP sensor; and CCT8 remains ADP-bound and is hardly involved in the ATPase-cycle in our experimental conditions; overall, yeast TRiC consumes nucleotide in a 2-ring positively coordinated manner. Our results depict a thorough picture of the TRiC conformational landscape and its allosteric transitions from the open to closed states in more structural detail and offer insights into TRiC subunit specificity in ATP consumption and ring closure, and potentially in substrate processing.	+
-		+
-	An ensemble of cryo-EM structures of TRiC reveal its conformational landscape and subunit specificity.,Jin M, Han W, Liu C, Zang Y, Li J, Wang F, Wang Y, Cong Y Proc Natl Acad Sci U S A. 2019 Sep 24;116(39):19513-19522. doi:, 10.1073/pnas.1903976116. Epub 2019 Sep 6. PMID:31492816<ref>PMID:31492816</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 6ks7" style="background-color:#fffaf0;"></div>~~	+
-	~~== References ==~~	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</SX>		</SX>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Saccharomyces cerevisiae ~~s288c~~]]	+	[[Category: Saccharomyces cerevisiae S288C]]
-	[[Category: Cong, Y]]	+	[[Category: Cong Y]]
-	[[Category: Jin, M]]	+	[[Category: Jin M]]
-	~~[[Category: Allosteric network]]~~	+
-	~~[[Category: Atpase cycle]]~~	+
-	~~[[Category: Chaperone]]~~	+
-	~~[[Category: Chaperonin tric/cct]]~~	+
-	~~[[Category: Conformational landscape]]~~	+
-	~~[[Category: Cryo-em~~]]	+

OCA at 02:30, 11 April 2020

OCA — Sat, 11 Apr 2020 02:30:21 GMT

←Older revision		Revision as of 02:30, 11 April 2020
Line 3:		Line 3:
	<SX load='6ks7' size='340' side='right' viewer='molstar' caption='[[6ks7]], [[Resolution\|resolution]] 4.62Å' scene=''>		<SX load='6ks7' size='340' side='right' viewer='molstar' caption='[[6ks7]], [[Resolution\|resolution]] 4.62Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6ks7]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KS7 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6KS7 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6ks7]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KS7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6KS7 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=6ks7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ks7 OCA], [http://pdbe.org/6ks7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ks7 RCSB], [http://www.ebi.ac.uk/pdbsum/6ks7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ks7 ProSAT]</span></td></tr>	+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6ks7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ks7 OCA], [http://pdbe.org/6ks7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ks7 RCSB], [http://www.ebi.ac.uk/pdbsum/6ks7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ks7 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 22:27, 6 March 2020

OCA — Fri, 06 Mar 2020 22:27:25 GMT

←Older revision		Revision as of 22:27, 6 March 2020
Line 1:		Line 1:

	==TRiC at 0.1 mM ADP-AlFx, Conformation 1, 0.1-C1==		==TRiC at 0.1 mM ADP-AlFx, Conformation 1, 0.1-C1==
-	<~~StructureSection~~ load='6ks7' size='340' side='right'caption='[[6ks7]], [[Resolution\|resolution]] 4.62Å' scene=''>	+	<SX load='6ks7' size='340' side='right' viewer='molstar' caption='[[6ks7]], [[Resolution\|resolution]] 4.62Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[6ks7]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KS7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6KS7 FirstGlance]. <br>		<table><tr><td colspan='2'>[[6ks7]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KS7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6KS7 FirstGlance]. <br>
Line 20:		Line 20:
	<references/>		<references/>
	__TOC__		__TOC__
-	</~~StructureSection~~>	+	</SX>
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Saccharomyces cerevisiae s288c]]		[[Category: Saccharomyces cerevisiae s288c]]

OCA at 06:10, 10 October 2019

OCA — Thu, 10 Oct 2019 06:10:23 GMT

←Older revision		Revision as of 06:10, 10 October 2019
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6ks7 is ~~ON HOLD~~	+	==TRiC at 0.1 mM ADP-AlFx, Conformation 1, 0.1-C1==
		+	<StructureSection load='6ks7' size='340' side='right'caption='[[6ks7]], [[Resolution\|resolution]] 4.62Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[6ks7]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KS7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6KS7 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=6ks7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ks7 OCA], [http://pdbe.org/6ks7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ks7 RCSB], [http://www.ebi.ac.uk/pdbsum/6ks7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ks7 ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/TCPE_YEAST TCPE_YEAST]] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation. [[http://www.uniprot.org/uniprot/TCPB_YEAST TCPB_YEAST]] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation. [[http://www.uniprot.org/uniprot/TCPG_YEAST TCPG_YEAST]] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation. [[http://www.uniprot.org/uniprot/TCPZ_YEAST TCPZ_YEAST]] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation. [[http://www.uniprot.org/uniprot/TCPA_YEAST TCPA_YEAST]] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation. [[http://www.uniprot.org/uniprot/TCPQ_YEAST TCPQ_YEAST]] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation (By similarity). [[http://www.uniprot.org/uniprot/TCPH_YEAST TCPH_YEAST]] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation (By similarity). [[http://www.uniprot.org/uniprot/TCPD_YEAST TCPD_YEAST]] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	TRiC/CCT assists the folding of approximately 10% of cytosolic proteins through an ATP-driven conformational cycle and is essential in maintaining protein homeostasis. Here, we determined an ensemble of cryo-electron microscopy (cryo-EM) structures of yeast TRiC at various nucleotide concentrations, with 4 open-state maps resolved at near-atomic resolutions, and a closed-state map at atomic resolution, revealing an extra layer of an unforeseen N-terminal allosteric network. We found that, during TRiC ring closure, the CCT7 subunit moves first, responding to nucleotide binding; CCT4 is the last to bind ATP, serving as an ATP sensor; and CCT8 remains ADP-bound and is hardly involved in the ATPase-cycle in our experimental conditions; overall, yeast TRiC consumes nucleotide in a 2-ring positively coordinated manner. Our results depict a thorough picture of the TRiC conformational landscape and its allosteric transitions from the open to closed states in more structural detail and offer insights into TRiC subunit specificity in ATP consumption and ring closure, and potentially in substrate processing.

-	~~Authors: Mingliang, J~~., ~~Yao~~, C.	+	An ensemble of cryo-EM structures of TRiC reveal its conformational landscape and subunit specificity.,Jin M, Han W, Liu C, Zang Y, Li J, Wang F, Wang Y, Cong Y Proc Natl Acad Sci U S A. 2019 Sep 24;116(39):19513-19522. doi:, 10.1073/pnas.1903976116. Epub 2019 Sep 6. PMID:31492816<ref>PMID:31492816</ref>

-	~~Description: TRiC at 0.1 mM ADP-AlFx~~, ~~Conformation 1, 0~~.1-C1	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
-	[[Category: ~~Yao~~, C]]	+	<div class="pdbe-citations 6ks7" style="background-color:#fffaf0;"></div>
-	[[Category: ~~Mingliang~~, J]]	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Saccharomyces cerevisiae s288c]]
		+	[[Category: Cong, Y]]
		+	[[Category: Jin, M]]
		+	[[Category: Allosteric network]]
		+	[[Category: Atpase cycle]]
		+	[[Category: Chaperone]]
		+	[[Category: Chaperonin tric/cct]]
		+	[[Category: Conformational landscape]]
		+	[[Category: Cryo-em]]

OCA: Protected "6ks7" [edit=sysop:move=sysop]

OCA — Wed, 28 Aug 2019 13:42:05 GMT

Protected "6ks7" [edit=sysop:move=sysop]

←Older revision

Revision as of 13:42, 28 August 2019

OCA: New page: '''Unreleased structure''' The entry 6ks7 is ON HOLD Authors: Mingliang, J., Yao, C. Description: TRiC at 0.1 mM ADP-AlFx, Conformation 1, 0.1-C1 Category: Unreleased Structures [[...

OCA — Wed, 28 Aug 2019 13:42:03 GMT

New page: '''Unreleased structure''' The entry 6ks7 is ON HOLD Authors: Mingliang, J., Yao, C. Description: TRiC at 0.1 mM ADP-AlFx, Conformation 1, 0.1-C1 Category: Unreleased Structures [[...

New page

'''Unreleased structure'''

The entry 6ks7 is ON HOLD

Authors: Mingliang, J., Yao, C.

Description: TRiC at 0.1 mM ADP-AlFx, Conformation 1, 0.1-C1
[[Category: Unreleased Structures]]
[[Category: Yao, C]]
[[Category: Mingliang, J]]