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6hxn

From Proteopedia

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Current revision (07:35, 1 May 2024) (edit) (undo)
 
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<StructureSection load='6hxn' size='340' side='right'caption='[[6hxn]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='6hxn' size='340' side='right'caption='[[6hxn]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6hxn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chlli Chlli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HXN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HXN FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6hxn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlorobium_limicola Chlorobium limicola]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HXN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HXN FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aclA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1092 CHLLI])</td></tr>
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<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>
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<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=6hxn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hxn OCA], [http://pdbe.org/6hxn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hxn RCSB], [http://www.ebi.ac.uk/pdbsum/6hxn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hxn ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6hxn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hxn OCA], [https://pdbe.org/6hxn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hxn RCSB], [https://www.ebi.ac.uk/pdbsum/6hxn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hxn ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q9AJC4_CHLLI Q9AJC4_CHLLI]
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6hxn" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Chlli]]
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[[Category: Chlorobium limicola]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Verschueren, K]]
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[[Category: Verschueren K]]
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[[Category: Verstraete, K]]
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[[Category: Verstraete K]]
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[[Category: Acetyl-coa]]
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[[Category: Atp citrate lyase]]
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[[Category: Central metabolism]]
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[[Category: Citrate shuttle]]
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[[Category: Citryl-coa]]
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[[Category: Lipogenesis]]
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[[Category: Lyase]]
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[[Category: Rtca cycle]]
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Current revision

Structure of the citryl-CoA lyase core module of Chlorobium limicola ATP citrate lyase (space group P3121)

PDB ID 6hxn

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