7f3x: Difference between revisions

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<StructureSection load='7f3x' size='340' side='right'caption='[[7f3x]], [[Resolution|resolution]] 3.57&Aring;' scene=''>
<StructureSection load='7f3x' size='340' side='right'caption='[[7f3x]], [[Resolution|resolution]] 3.57&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7f3x]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7F3X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7F3X FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7F3X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7F3X FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LAP:[2-((1-OXODODECANOXY-(2-HYDROXY-3-PROPANYL))-PHOSPHONATE-OXY)-ETHYL]-TRIMETHYLAMMONIUM'>LAP</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.57&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LAP:[2-((1-OXODODECANOXY-(2-HYDROXY-3-PROPANYL))-PHOSPHONATE-OXY)-ETHYL]-TRIMETHYLAMMONIUM'>LAP</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=7f3x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7f3x OCA], [https://pdbe.org/7f3x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7f3x RCSB], [https://www.ebi.ac.uk/pdbsum/7f3x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7f3x ProSAT]</span></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=7f3x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7f3x OCA], [https://pdbe.org/7f3x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7f3x RCSB], [https://www.ebi.ac.uk/pdbsum/7f3x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7f3x ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
As the major component of cell membranes, phosphatidylcholine (PC) is synthesized de novo in the Kennedy pathway and then undergoes extensive deacylation-reacylation remodeling via Lands' cycle. The re-acylation is catalyzed by lysophosphatidylcholine acyltransferase (LPCAT) and among the four LPCAT members in human, the LPCAT3 preferentially introduces polyunsaturated acyl onto the sn-2 position of lysophosphatidylcholine, thereby modulating the membrane fluidity and membrane protein functions therein. Combining the x-ray crystallography and the cryo-electron microscopy, we determined the structures of LPCAT3 in apo-, acyl donor-bound, and acyl receptor-bound states. A reaction chamber was revealed in the LPCAT3 structure where the lysophosphatidylcholine and arachidonoyl-CoA were positioned in two tunnels connected near to the catalytic center. A side pocket was found expanding the tunnel for the arachidonoyl CoA and holding the main body of arachidonoyl. The structural and functional analysis provides the basis for the re-acylation of lysophosphatidylcholine and the substrate preference during the reactions.
The structural basis for the phospholipid remodeling by lysophosphatidylcholine acyltransferase 3.,Zhang Q, Yao D, Rao B, Jian L, Chen Y, Hu K, Xia Y, Li S, Shen Y, Qin A, Zhao J, Zhou L, Lei M, Jiang XC, Cao Y Nat Commun. 2021 Nov 25;12(1):6869. doi: 10.1038/s41467-021-27244-1. PMID:34824256<ref>PMID:34824256</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7f3x" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Cao, Y]]
[[Category: Cao Y]]
[[Category: Chen, Y]]
[[Category: Chen Y]]
[[Category: Hu, K]]
[[Category: Hu K]]
[[Category: Jian, L]]
[[Category: Jian L]]
[[Category: Li, S]]
[[Category: Li S]]
[[Category: Rao, B]]
[[Category: Rao B]]
[[Category: Shen, Y]]
[[Category: Shen Y]]
[[Category: Xia, Y]]
[[Category: Xia Y]]
[[Category: Yao, D]]
[[Category: Yao D]]
[[Category: Zhang, Q]]
[[Category: Zhang Q]]
[[Category: Cryo-em]]
[[Category: Lpcat3]]
[[Category: Membrane-bound o-acyltransferase]]
[[Category: Phospholipid remodeling]]
[[Category: Transferase]]

Latest revision as of 05:09, 12 June 2024

Lysophospholipid acyltransferase LPCAT3 in complex with lysophosphatidylcholine

7f3x, resolution 3.57Å

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