6hxp - Revision history

OCA at 07:35, 1 May 2024

OCA — Wed, 01 May 2024 07:35:12 GMT

←Older revision		Revision as of 07:35, 1 May 2024
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	<StructureSection load='6hxp' size='340' side='right'caption='[[6hxp]], [[Resolution\|resolution]] 1.45Å' scene=''>		<StructureSection load='6hxp' size='340' side='right'caption='[[6hxp]], [[Resolution\|resolution]] 1.45Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6hxp]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Dsm_6534 Dsm 6534~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HXP OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6HXP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6hxp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hydrogenobacter_thermophilus Hydrogenobacter thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HXP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HXP FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><scene name~~=~~'pdbligand=COA:COENZYME+A'>COA</scene~~>, ~~<scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.45Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~ccl ([http~~:/~~/www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode~~=~~Info&srchmode~~=~~5&id=940 DSM 6534])~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6hxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hxp OCA], [~~http~~://pdbe.org/6hxp PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6hxp RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6hxp PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6hxp 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=6hxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hxp OCA], [https://pdbe.org/6hxp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hxp RCSB], [https://www.ebi.ac.uk/pdbsum/6hxp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hxp ProSAT]</span></td></tr>
	</table>		</table>
-	~~<div style~~=~~"background-color:#fffaf0;">~~	+	== Function ==
-	=~~= Publication Abstract from PubMed~~ ==	+	[https://www.uniprot.org/uniprot/Q75VX1_HYDTH Q75VX1_HYDTH]
-	Across different kingdoms of life, ATP citrate lyase (ACLY, also known as ACL) catalyses the ATP-dependent and coenzyme A (CoA)-dependent conversion of citrate, a metabolic product of the Krebs cycle, to oxaloacetate and the high-energy biosynthetic precursor acetyl-CoA(1). The latter fuels pivotal biochemical reactions such as the synthesis of fatty acids, cholesterol and acetylcholine(2), and the acetylation of histones and proteins(3,4). In autotrophic prokaryotes, ACLY is a hallmark enzyme of the reverse Krebs cycle (also known as the reductive tricarboxylic acid cycle), which fixates two molecules of carbon dioxide in acetyl-CoA(5,6). In humans, ACLY links carbohydrate and lipid metabolism and is strongly expressed in liver and adipose tissue(1) and in cholinergic neurons(2,7). The structural basis of the function of ACLY remains unknown. Here we report high-resolution crystal structures of bacterial, archaeal and human ACLY, and use distinct substrate-bound states to link the conformational plasticity of ACLY to its multistep catalytic itinerary. Such detailed insights will provide the framework for targeting human ACLY in cancer(8-11) and hyperlipidaemia(12,13). Our structural studies also unmask a fundamental evolutionary relationship that links citrate synthase, the first enzyme of the oxidative Krebs cycle, to an ancestral tetrameric citryl-CoA lyase module that operates in the reverse Krebs cycle. This molecular transition marked a key step in the evolution of metabolism on Earth.	+
-		+
-	Structure of ATP citrate lyase and the origin of citrate synthase in the Krebs cycle.,Verschueren KHG, Blanchet C, Felix J, Dansercoer A, De Vos D, Bloch Y, Van Beeumen J, Svergun D, Gutsche I, Savvides SN, Verstraete K Nature. 2019 Apr 3. pii: ~~10.1038~~/~~s41586-019-1095-5. doi:, 10.1038~~/~~s41586-019-1095-5~~. ~~PMID:30944476<ref>PMID:30944476</ref>~~	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U~~.~~S. National Library of Medicine.<br>~~	+
-	</~~div>~~	+
-	~~<div class="pdbe-citations 6hxp" style="background-color:#fffaf0;"></div>~~	+
-	~~== References ==~~	+
-	~~<references~~/>	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Dsm 6534~~]]	+	[[Category: Hydrogenobacter thermophilus]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Verschueren, K]]	+	[[Category: Verschueren K]]
-	[[Category: Verstraete, K]]	+	[[Category: Verstraete K]]
-	~~[[Category: Acetyl-coa]]~~	+
-	~~[[Category: Atp citrate lyase]]~~	+
-	~~[[Category: Central metabolism]]~~	+
-	~~[[Category: Citrate shuttle]]~~	+
-	~~[[Category: Citryl-coa]]~~	+
-	~~[[Category: Lipogenesis]]~~	+
-	~~[[Category: Lyase]]~~	+
-	~~[[Category: Rtca cycle~~]]	+

OCA at 06:54, 17 April 2019

OCA — Wed, 17 Apr 2019 06:54:03 GMT

←Older revision		Revision as of 06:54, 17 April 2019
Line 3:		Line 3:
	<StructureSection load='6hxp' size='340' side='right'caption='[[6hxp]], [[Resolution\|resolution]] 1.45Å' scene=''>		<StructureSection load='6hxp' size='340' side='right'caption='[[6hxp]], [[Resolution\|resolution]] 1.45Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6hxp]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HXP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HXP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6hxp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Dsm_6534 Dsm 6534]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HXP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HXP FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ccl ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=940 DSM 6534])</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=6hxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hxp OCA], [http://pdbe.org/6hxp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hxp RCSB], [http://www.ebi.ac.uk/pdbsum/6hxp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hxp 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=6hxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hxp OCA], [http://pdbe.org/6hxp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hxp RCSB], [http://www.ebi.ac.uk/pdbsum/6hxp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hxp ProSAT]</span></td></tr>
	</table>		</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Across different kingdoms of life, ATP citrate lyase (ACLY, also known as ACL) catalyses the ATP-dependent and coenzyme A (CoA)-dependent conversion of citrate, a metabolic product of the Krebs cycle, to oxaloacetate and the high-energy biosynthetic precursor acetyl-CoA(1). The latter fuels pivotal biochemical reactions such as the synthesis of fatty acids, cholesterol and acetylcholine(2), and the acetylation of histones and proteins(3,4). In autotrophic prokaryotes, ACLY is a hallmark enzyme of the reverse Krebs cycle (also known as the reductive tricarboxylic acid cycle), which fixates two molecules of carbon dioxide in acetyl-CoA(5,6). In humans, ACLY links carbohydrate and lipid metabolism and is strongly expressed in liver and adipose tissue(1) and in cholinergic neurons(2,7). The structural basis of the function of ACLY remains unknown. Here we report high-resolution crystal structures of bacterial, archaeal and human ACLY, and use distinct substrate-bound states to link the conformational plasticity of ACLY to its multistep catalytic itinerary. Such detailed insights will provide the framework for targeting human ACLY in cancer(8-11) and hyperlipidaemia(12,13). Our structural studies also unmask a fundamental evolutionary relationship that links citrate synthase, the first enzyme of the oxidative Krebs cycle, to an ancestral tetrameric citryl-CoA lyase module that operates in the reverse Krebs cycle. This molecular transition marked a key step in the evolution of metabolism on Earth.
		+
		+	Structure of ATP citrate lyase and the origin of citrate synthase in the Krebs cycle.,Verschueren KHG, Blanchet C, Felix J, Dansercoer A, De Vos D, Bloch Y, Van Beeumen J, Svergun D, Gutsche I, Savvides SN, Verstraete K Nature. 2019 Apr 3. pii: 10.1038/s41586-019-1095-5. doi:, 10.1038/s41586-019-1095-5. PMID:30944476<ref>PMID:30944476</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6hxp" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Dsm 6534]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Verschueren, K]]		[[Category: Verschueren, K]]

OCA at 07:21, 10 April 2019

OCA — Wed, 10 Apr 2019 07:21:17 GMT

←Older revision		Revision as of 07:21, 10 April 2019
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6hxp ~~is ON HOLD until Paper Publication~~	+	==Structure of citryl-CoA lyase from Hydrogenobacter thermophilus==
-		+	<StructureSection load='6hxp' size='340' side='right'caption='[[6hxp]], [[Resolution\|resolution]] 1.45Å' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[6hxp]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HXP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HXP FirstGlance]. <br>
-	~~Description~~:	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	<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=6hxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hxp OCA], [http://pdbe.org/6hxp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hxp RCSB], [http://www.ebi.ac.uk/pdbsum/6hxp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hxp ProSAT]</span></td></tr>
		+	</table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Verschueren, K]]
		+	[[Category: Verstraete, K]]
		+	[[Category: Acetyl-coa]]
		+	[[Category: Atp citrate lyase]]
		+	[[Category: Central metabolism]]
		+	[[Category: Citrate shuttle]]
		+	[[Category: Citryl-coa]]
		+	[[Category: Lipogenesis]]
		+	[[Category: Lyase]]
		+	[[Category: Rtca cycle]]

OCA at 09:52, 13 March 2019

OCA — Wed, 13 Mar 2019 09:52:17 GMT

←Older revision		Revision as of 09:52, 13 March 2019
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors:		Authors:

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

OCA — Wed, 24 Oct 2018 04:16:00 GMT

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

←Older revision

Revision as of 04:16, 24 October 2018

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

OCA — Wed, 24 Oct 2018 04:15:59 GMT

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

New page

'''Unreleased structure'''

The entry 6hxp is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]