6tmx - Revision history

OCA at 10:18, 22 May 2024

OCA — Wed, 22 May 2024 10:18:35 GMT

←Older revision		Revision as of 10:18, 22 May 2024
Line 3:		Line 3:
	<StructureSection load='6tmx' size='340' side='right'caption='[[6tmx]], [[Resolution\|resolution]] 5.80Å' scene=''>		<StructureSection load='6tmx' size='340' side='right'caption='[[6tmx]], [[Resolution\|resolution]] 5.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6tmx]] is a 14 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Pseudomonas_phage_el~~ Pseudomonas phage el]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TMX OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=6TMX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6tmx]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_phage_EL Pseudomonas phage EL]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TMX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TMX FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>~~</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]] 5.8Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[6tmt\|6tmt]], [[6tmu\|6tmu]], [[6tmv\|6tmv]], [[6tmw\|6tmw]]~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=6tmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tmx OCA], [~~http~~://pdbe.org/6tmx PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6tmx RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6tmx PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6tmx 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=6tmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tmx OCA], [https://pdbe.org/6tmx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tmx RCSB], [https://www.ebi.ac.uk/pdbsum/6tmx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tmx ProSAT]</span></td></tr>
	</table>		</table>
-	~~<div style~~=~~"background-color:#fffaf0;">~~	+	== Function ==
-	=~~= Publication Abstract from PubMed~~ ==	+	[https://www.uniprot.org/uniprot/Q2Z0T5_9CAUD Q2Z0T5_9CAUD]
-	Chaperonins are ubiquitous molecular chaperones found in all domains of life. They form ring-shaped complexes that assist in the folding of substrate proteins in an ATP-dependent reaction cycle. Key to the folding cycle is the transient encapsulation of substrate proteins by the chaperonin. Here we present a structural and functional characterization of the chaperonin gp146 (EL) from the phage EL of Pseudomonas aeruginosa. EL, an evolutionarily distant homolog of bacterial GroEL, is active in ATP hydrolysis and prevents the aggregation of denatured protein in a nucleotide-dependent manner. However, EL failed to refold the encapsulation-dependent model substrate rhodanese and did not interact with E. coli GroES, the lid-shaped co-chaperone of GroEL. EL forms tetradecameric double-ring complexes, which dissociate into single rings in the presence of ATP. Crystal structures of EL (at 3.54 and 4.03 A) in presence of ATP*BeFx revealed two distinct single-ring conformational states, both with open access to the ring cavity. One state showed uniform ATP-bound subunit conformations (symmetric state), whereas the second combined distinct ATP- and ADP-bound subunit conformations (asymmetric state). Cryo-electron microscopy of apo-EL revealed a double-ring structure composed of rings in the asymmetric state (3.45 A resolution). We propose that the phage chaperonin undergoes nucleotide-dependent conformational switching between double- and single rings and functions in aggregation prevention without substrate protein encapsulation. Thus, EL may represent an evolutionarily more ancient chaperonin prior to acquisition of the encapsulation mechanism.	+
-		+
-	~~Structure and conformational cycle of a bacteriophage-encoded chaperonin.,Bracher A, Paul SS, Wang H, Wischnewski N, Hartl FU, Hayer-Hartl M PLoS One. 2020 Apr 27;15(4)~~:~~e0230090. doi: 10.1371~~/~~journal.pone.0230090., eCollection 2020. PMID:32339190<ref>PMID:32339190<~~/~~ref>~~	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U~~.S. ~~National Library of Medicine.<br>~~	+
-	</~~div>~~	+
-	~~<div class="pdbe-citations 6tmx" style="background-color:#fffaf0;"></div>~~	+
-	~~== References ==~~	+
-	~~<references~~/>	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Pseudomonas phage el]]	+	[[Category: Pseudomonas phage EL]]
-	[[Category: Bracher, A]]	+	[[Category: Bracher A]]
-	[[Category: Hartl~~, F U~~]]	+	[[Category: Hartl FU]]
-	[[Category: Hayer-Hartl, M]]	+	[[Category: Hayer-Hartl M]]
-	[[Category: Paul~~, S S~~]]	+	[[Category: Paul SS]]
-	[[Category: Wang, H]]	+	[[Category: Wang H]]
-	[[Category: Wischnewski, N]]	+	[[Category: Wischnewski N]]
-	~~[[Category: Atpase]]~~	+
-	~~[[Category: Chaperone]]~~	+
-	~~[[Category: Chaperonin]]~~	+
-	~~[[Category: Molecular chaperone~~]]	+

OCA at 06:34, 6 May 2020

OCA — Wed, 06 May 2020 06:34:37 GMT

←Older revision		Revision as of 06:34, 6 May 2020
Line 1:		Line 1:

	==Structure of the chaperonin gp146 from the bacteriophage EL (Pseudomonas aeruginosa) in complex with ATPgammaS==		==Structure of the chaperonin gp146 from the bacteriophage EL (Pseudomonas aeruginosa) in complex with ATPgammaS==
-	<StructureSection load='6tmx' size='340' side='right'caption='[[6tmx]]' scene=''>	+	<StructureSection load='6tmx' size='340' side='right'caption='[[6tmx]], [[Resolution\|resolution]] 5.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TMX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6TMX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6tmx]] is a 14 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_phage_el Pseudomonas phage el]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TMX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6TMX 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=6tmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tmx OCA], [http://pdbe.org/6tmx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tmx RCSB], [http://www.ebi.ac.uk/pdbsum/6tmx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tmx ProSAT]</span></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[6tmt\|6tmt]], [[6tmu\|6tmu]], [[6tmv\|6tmv]], [[6tmw\|6tmw]]</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=6tmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tmx OCA], [http://pdbe.org/6tmx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tmx RCSB], [http://www.ebi.ac.uk/pdbsum/6tmx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tmx ProSAT]</span></td></tr>
	</table>		</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Chaperonins are ubiquitous molecular chaperones found in all domains of life. They form ring-shaped complexes that assist in the folding of substrate proteins in an ATP-dependent reaction cycle. Key to the folding cycle is the transient encapsulation of substrate proteins by the chaperonin. Here we present a structural and functional characterization of the chaperonin gp146 (EL) from the phage EL of Pseudomonas aeruginosa. EL, an evolutionarily distant homolog of bacterial GroEL, is active in ATP hydrolysis and prevents the aggregation of denatured protein in a nucleotide-dependent manner. However, EL failed to refold the encapsulation-dependent model substrate rhodanese and did not interact with E. coli GroES, the lid-shaped co-chaperone of GroEL. EL forms tetradecameric double-ring complexes, which dissociate into single rings in the presence of ATP. Crystal structures of EL (at 3.54 and 4.03 A) in presence of ATP*BeFx revealed two distinct single-ring conformational states, both with open access to the ring cavity. One state showed uniform ATP-bound subunit conformations (symmetric state), whereas the second combined distinct ATP- and ADP-bound subunit conformations (asymmetric state). Cryo-electron microscopy of apo-EL revealed a double-ring structure composed of rings in the asymmetric state (3.45 A resolution). We propose that the phage chaperonin undergoes nucleotide-dependent conformational switching between double- and single rings and functions in aggregation prevention without substrate protein encapsulation. Thus, EL may represent an evolutionarily more ancient chaperonin prior to acquisition of the encapsulation mechanism.
		+
		+	Structure and conformational cycle of a bacteriophage-encoded chaperonin.,Bracher A, Paul SS, Wang H, Wischnewski N, Hartl FU, Hayer-Hartl M PLoS One. 2020 Apr 27;15(4):e0230090. doi: 10.1371/journal.pone.0230090., eCollection 2020. PMID:32339190<ref>PMID:32339190</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6tmx" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Bracher A]]	+	[[Category: Pseudomonas phage el]]
-	[[Category: Hartl FU]]	+	[[Category: Bracher, A]]
-	[[Category: Hayer-Hartl M]]	+	[[Category: Hartl, F U]]
-	[[Category: Paul SS]]	+	[[Category: Hayer-Hartl, M]]
-	[[Category: Wang H]]	+	[[Category: Paul, S S]]
-	[[Category: Wischnewski N]]	+	[[Category: Wang, H]]
		+	[[Category: Wischnewski, N]]
		+	[[Category: Atpase]]
		+	[[Category: Chaperone]]
		+	[[Category: Chaperonin]]
		+	[[Category: Molecular chaperone]]

OCA at 05:45, 22 April 2020

OCA — Wed, 22 Apr 2020 05:45:29 GMT

←Older revision		Revision as of 05:45, 22 April 2020
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6tmx is ~~ON HOLD until Paper Publication~~	+	==Structure of the chaperonin gp146 from the bacteriophage EL (Pseudomonas aeruginosa) in complex with ATPgammaS==
-		+	<StructureSection load='6tmx' size='340' side='right'caption='[[6tmx]]' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TMX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6TMX FirstGlance]. <br>
-	~~Description~~:	+	</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=6tmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tmx OCA], [http://pdbe.org/6tmx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tmx RCSB], [http://www.ebi.ac.uk/pdbsum/6tmx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tmx ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	</table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Bracher A]]
		+	[[Category: Hartl FU]]
		+	[[Category: Hayer-Hartl M]]
		+	[[Category: Paul SS]]
		+	[[Category: Wang H]]
		+	[[Category: Wischnewski N]]

OCA at 05:50, 18 December 2019

OCA — Wed, 18 Dec 2019 05:50:33 GMT

←Older revision		Revision as of 05:50, 18 December 2019
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors:		Authors:

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

OCA — Wed, 11 Dec 2019 13:40:27 GMT

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

←Older revision

Revision as of 13:40, 11 December 2019

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

OCA — Wed, 11 Dec 2019 13:40:26 GMT

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

New page

'''Unreleased structure'''

The entry 6tmx is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]