3pff: Difference between revisions

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[[Image:3pff.png|left|200px]]


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==Truncated human atp-citrate lyase with ADP and tartrate bound==
The line below this paragraph, containing "STRUCTURE_3pff", creates the "Structure Box" on the page.
<StructureSection load='3pff' size='340' side='right'caption='[[3pff]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3pff]] is a 1 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=3PFF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PFF FirstGlance]. <br>
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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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr>
{{STRUCTURE_3pff|  PDB=3pff  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3pff FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pff OCA], [https://pdbe.org/3pff PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pff RCSB], [https://www.ebi.ac.uk/pdbsum/3pff PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pff 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>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Human ATP-citrate lyase (EC 2.3.3.8) is the cytoplasmic enzyme that catalyzes the production of acetyl-CoA from citrate, CoA and ATP. The amino-terminal portion of the enzyme, containing residues 1-817, was crystallized in the presence of tartrate, ATP and magnesium ions. The crystals diffracted to 2.3 A resolution. The structure shows ADP-Mg(2+) bound to the domain that possesses the ATP-grasp fold. The structure demonstrates that this crystal form could be used to investigate the structures of complexes with inhibitors of ATP-citrate lyase that bind at either the citrate- or ATP-binding site.


===Truncated human atp-citrate lyase with ADP and tartrate bound===
ADP-Mg2+ bound to the ATP-grasp domain of ATP-citrate lyase.,Sun T, Hayakawa K, Fraser ME Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Oct 1;67(Pt 10):1168-72., Epub 2011 Sep 24. PMID:22102020<ref>PMID:22102020</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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{{ABSTRACT_PUBMED_22102020}}
 
==About this Structure==
[[3pff]] is a 1 chain structure of [[ATP-citrate synthase]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PFF OCA].


==See Also==
==See Also==
*[[ATP-citrate synthase|ATP-citrate synthase]]
*[[ATP-citrate synthase|ATP-citrate synthase]]
 
*[[ATP-citrate synthase 3D structures|ATP-citrate synthase 3D structures]]
==Reference==
== References ==
<ref group="xtra">PMID:022102020</ref><references group="xtra"/>
<references/>
[[Category: ATP citrate synthase]]
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Fraser, M E.]]
[[Category: Large Structures]]
[[Category: Sun, T.]]
[[Category: Fraser ME]]
[[Category: Atp-grasp]]
[[Category: Sun T]]
[[Category: Lyase]]
[[Category: Organic acid]]
[[Category: Phosphohistidine]]
[[Category: Transferase]]

Latest revision as of 12:53, 6 September 2023

Truncated human atp-citrate lyase with ADP and tartrate boundTruncated human atp-citrate lyase with ADP and tartrate bound

Structural highlights

3pff is a 1 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 2.3Å
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]

Publication Abstract from PubMed

Human ATP-citrate lyase (EC 2.3.3.8) is the cytoplasmic enzyme that catalyzes the production of acetyl-CoA from citrate, CoA and ATP. The amino-terminal portion of the enzyme, containing residues 1-817, was crystallized in the presence of tartrate, ATP and magnesium ions. The crystals diffracted to 2.3 A resolution. The structure shows ADP-Mg(2+) bound to the domain that possesses the ATP-grasp fold. The structure demonstrates that this crystal form could be used to investigate the structures of complexes with inhibitors of ATP-citrate lyase that bind at either the citrate- or ATP-binding site.

ADP-Mg2+ bound to the ATP-grasp domain of ATP-citrate lyase.,Sun T, Hayakawa K, Fraser ME Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Oct 1;67(Pt 10):1168-72., Epub 2011 Sep 24. PMID:22102020[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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
  2. ↑ Sun T, Hayakawa K, Fraser ME. ADP-Mg2+ bound to the ATP-grasp domain of ATP-citrate lyase. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Oct 1;67(Pt 10):1168-72., Epub 2011 Sep 24. PMID:22102020 doi:10.1107/S1744309111028363

3pff, resolution 2.30Å

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