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5teq

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==C20S C293G MUTANT N-TERMINAL HUMAN ATP CITRATE LYASE BOUND TO CITRATE==
==C20S C293G MUTANT N-TERMINAL HUMAN ATP CITRATE LYASE BOUND TO CITRATE==
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<StructureSection load='5teq' size='340' side='right' caption='[[5teq]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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<StructureSection load='5teq' size='340' side='right'caption='[[5teq]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5teq]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TEQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TEQ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5teq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TEQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TEQ 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=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.3&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5tes|5tes]], [[5tet|5tet]]</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=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/ATP_citrate_synthase ATP citrate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.3.8 2.3.3.8] </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=5teq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5teq OCA], [https://pdbe.org/5teq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5teq RCSB], [https://www.ebi.ac.uk/pdbsum/5teq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5teq ProSAT]</span></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=5teq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5teq OCA], [http://pdbe.org/5teq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5teq RCSB], [http://www.ebi.ac.uk/pdbsum/5teq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5teq ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ACLY_HUMAN ACLY_HUMAN]] ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. Has a central role in de novo lipid synthesis. In nervous tissue it may be involved in the biosynthesis of acetylcholine.<ref>PMID:23932781</ref>
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[https://www.uniprot.org/uniprot/ACLY_HUMAN ACLY_HUMAN] ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. Has a central role in de novo lipid synthesis. In nervous tissue it may be involved in the biosynthesis of acetylcholine.<ref>PMID:23932781</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Hydroxycitrate from the fruit of Garcinia cambogia [i.e. (2S,3S)-2-hydroxycitrate] is the best-known inhibitor of ATP-citrate lyase. Well diffracting crystals showing how the inhibitor binds to human ATP-citrate lyase were grown by modifying the protein. The protein was modified by introducing cleavage sites for Tobacco etch virus protease on either side of a disordered linker. The protein crystallized consisted of residues 2-425-ENLYFQ and S-488-810 of human ATP-citrate lyase. (2S,3S)-2-Hydroxycitrate binds in the same orientation as citrate, but the citrate-binding domain (residues 248-421) adopts a different orientation with respect to the rest of the protein (residues 4-247, 490-746 and 748-809) from that previously seen. For the first time, electron density was evident for the loop that contains His760, which is phosphorylated as part of the catalytic mechanism. The pro-S carboxylate of (2S,3S)-2-hydroxycitrate is available to accept a phosphoryl group from His760. However, when co-crystals were grown with ATP and magnesium ions as well as either the inhibitor or citrate, Mg2+-ADP was bound and His760 was phosphorylated. The phosphoryl group was not transferred to the organic acid. This led to the interpretation that the active site is trapped in an open conformation. The strategy of designing cleavage sites to remove disordered residues could be useful in determining the crystal structures of other proteins.
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Binding of hydroxycitrate to human ATP-citrate lyase.,Hu J, Komakula A, Fraser ME Acta Crystallogr D Struct Biol. 2017 Aug 1;73(Pt 8):660-671. doi:, 10.1107/S2059798317009871. Epub 2017 Jul 28. PMID:28777081<ref>PMID:28777081</ref>
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==See Also==
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*[[ATP-citrate synthase 3D structures|ATP-citrate synthase 3D structures]]
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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 5teq" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: ATP citrate synthase]]
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[[Category: Homo sapiens]]
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[[Category: Fraser, M E]]
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[[Category: Large Structures]]
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[[Category: Hu, J]]
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[[Category: Fraser ME]]
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[[Category: Atp-grasp fold]]
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[[Category: Hu J]]
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[[Category: Citrate binding]]
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[[Category: Transferase]]
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Current revision

C20S C293G MUTANT N-TERMINAL HUMAN ATP CITRATE LYASE BOUND TO CITRATE

PDB ID 5teq

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