6nzy
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structural Determination of the Carboxy-terminal portion of ATP-citrate lyase== | |
| + | <StructureSection load='6nzy' size='340' side='right'caption='[[6nzy]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6nzy]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NZY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NZY FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=6nzy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nzy OCA], [http://pdbe.org/6nzy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nzy RCSB], [http://www.ebi.ac.uk/pdbsum/6nzy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nzy ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | ATP-citrate lyase (ACLY) catalyzes production of acetyl-CoA and oxaloacetate from CoA and citrate using ATP. In humans, this cytoplasmic enzyme connects energy metabolism from carbohydrates to the production of lipids. In certain bacteria, ACLY is used to fix carbon in the reductive tricarboxylic acid cycle. The carboxy(C)-terminal portion of ACLY shows sequence similarity to citrate synthase of the tricarboxylic acid cycle. To investigate the roles of residues of ACLY equivalent to active site residues of citrate synthase, these residues in ACLY from Chlorobium limicola were mutated, and the proteins were investigated using kinetics assays and biophysical techniques. To obtain the crystal structure of the C-terminal portion of ACLY, full-length C. limicola ACLY was cleaved, first non-specifically with chymotrypsin and subsequently with Tobacco Etch Virus protease. Crystals of the C-terminal portion diffracted to high resolution, providing structures that show the positions of active site residues and how ACLY tetramerizes. | ||
| - | + | Identification of the active site residues in ATP-citrate lyase's carboxy-terminal portion.,Nguyen VH, Singh N, Medina A, Uson I, Fraser ME Protein Sci. 2019 Oct;28(10):1840-1849. doi: 10.1002/pro.3708. Epub 2019 Aug 27. PMID:31411782<ref>PMID:31411782</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Nguyen, V | + | <div class="pdbe-citations 6nzy" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Fraser, M E]] | ||
| + | [[Category: Nguyen, V H]] | ||
| + | [[Category: Acetyl-coa]] | ||
| + | [[Category: Acyl-coa synthetase]] | ||
| + | [[Category: Carboxy-terminal portion]] | ||
| + | [[Category: Lyase]] | ||
Revision as of 07:45, 18 December 2019
Structural Determination of the Carboxy-terminal portion of ATP-citrate lyase
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