5tdf: Difference between revisions

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'''Unreleased structure'''


The entry 5tdf is ON HOLD  until Paper Publication
==TEV Cleaved Human ATP Citrate Lyase Bound to 4S hydroxycitrate==
<StructureSection load='5tdf' size='340' side='right'caption='[[5tdf]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5tdf]] 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=5TDF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TDF FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7A3:3-C-carboxy-2-deoxy-D-erythro-pentaric+acid'>7A3</scene>, <scene name='pdbligand=ADE:ADENINE'>ADE</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NEP:N1-PHOSPHONOHISTIDINE'>NEP</scene></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=5tdf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tdf OCA], [https://pdbe.org/5tdf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tdf RCSB], [https://www.ebi.ac.uk/pdbsum/5tdf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tdf ProSAT]</span></td></tr>
</table>
== Function ==
[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>


Authors: Hu, J., Fraser, M.E., Komakula, A.
==See Also==
 
*[[ATP-citrate synthase 3D structures|ATP-citrate synthase 3D structures]]
Description: TEV Cleaved Human ATP Citrate Lyase Bound to Citrate
== References ==
[[Category: Unreleased Structures]]
<references/>
[[Category: Komakula, A]]
__TOC__
[[Category: Fraser, M.E]]
</StructureSection>
[[Category: Hu, J]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Fraser ME]]
[[Category: Hu J]]

Latest revision as of 18:40, 6 March 2024

TEV Cleaved Human ATP Citrate Lyase Bound to 4S hydroxycitrateTEV Cleaved Human ATP Citrate Lyase Bound to 4S hydroxycitrate

Structural highlights

5tdf is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:, , , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1]

See Also

References

  1. ↑ Lin R, Tao R, Gao X, Li T, Zhou X, Guan KL, Xiong Y, Lei QY. Acetylation stabilizes ATP-citrate lyase to promote lipid biosynthesis and tumor growth. Mol Cell. 2013 Aug 22;51(4):506-18. doi: 10.1016/j.molcel.2013.07.002. Epub 2013 , Aug 8. PMID:23932781 doi:http://dx.doi.org/10.1016/j.molcel.2013.07.002

5tdf, resolution 1.80Å

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