|Entry||Database: PDB / ID: 7f40|
|Title||Lysophospholipid acyltransferase LPCAT3 in a complex with Arachidonoyl-CoA|
|Keywords||TRANSFERASE / Lysophospholipid Acyltransferase / LPCAT3 / membrane-bound O-acyltransferase / cryo-EM|
|Function / homology|
Function and homology information
positive regulation of triglyceride transport / positive regulation of sterol regulatory element binding protein cleavage / 1-acylglycerophosphoserine O-acyltransferase activity / 1-acylglycerophosphoethanolamine O-acyltransferase activity / lysophospholipid acyltransferase activity / Acyl chain remodelling of PC / Acyl chain remodelling of PS / Acyl chain remodelling of PE / positive regulation of intestinal cholesterol absorption / chylomicron assembly ...positive regulation of triglyceride transport / positive regulation of sterol regulatory element binding protein cleavage / 1-acylglycerophosphoserine O-acyltransferase activity / 1-acylglycerophosphoethanolamine O-acyltransferase activity / lysophospholipid acyltransferase activity / Acyl chain remodelling of PC / Acyl chain remodelling of PS / Acyl chain remodelling of PE / positive regulation of intestinal cholesterol absorption / chylomicron assembly / 1-acylglycerophosphocholine O-acyltransferase activity / phosphatidylserine acyl-chain remodeling / endoplasmic reticulum membrane organization / phosphatidylethanolamine acyl-chain remodeling / lipid modification / regulation of cholesterol biosynthetic process / intestinal stem cell homeostasis / phosphatidylcholine acyl-chain remodeling / negative regulation of response to endoplasmic reticulum stress / very-low-density lipoprotein particle assembly / phosphatidylcholine biosynthetic process / acyltransferase activity / negative regulation of inflammatory response / endoplasmic reticulum membrane / membrane / integral component of membrane
Similarity search - Function
MBOAT, membrane-bound O-acyltransferase family / Membrane bound O-acyl transferase, MBOAT
Similarity search - Domain/homology
Chem-3IX / 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE / Uncharacterized protein
Similarity search - Component
|Biological species||Gallus gallus (chicken)|
|Method||ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.49 Å|
|Authors||Zhang, Q. / Yao, D. / Rao, B. / Li, S. / Jian, L. / Chen, Y. / Hu, K. / Xia, Y. / Shen, Y. / Cao, Y.|
|Funding support|| China, 2items |
|Citation||Journal: Nat Commun / Year: 2021|
Title: The structural basis for the phospholipid remodeling by lysophosphatidylcholine acyltransferase 3.
Authors: Qing Zhang / Deqiang Yao / Bing Rao / Liyan Jian / Yang Chen / Kexin Hu / Ying Xia / Shaobai Li / Yafeng Shen / An Qin / Jie Zhao / Lu Zhou / Ming Lei / Xian-Cheng Jiang / Yu Cao /
Abstract: 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 ...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.
|Structure viewer||Molecule: |
Downloads & links
Mass: 57265.070 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Gallus gallus (chicken) / Gene: LPCAT3 / Plasmid: pcDNA3.4 / Cell line (production host): Expi293F / Production host: Homo sapiens (human) / References: UniProt: A0A1L1RNG8
Mass: 1053.986 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C41H66N7O17P3S / Feature type: SUBJECT OF INVESTIGATION
Mass: 787.121 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C44H85NO8P / Comment: DOPC, phospholipid*YM
|Has ligand of interest||Y|
|Experiment||Method: ELECTRON MICROSCOPY|
|EM experiment||Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction|
|Component||Name: Lysophospholipid acyltransferase 5 / Type: COMPLEX / Entity ID: #1 / Source: RECOMBINANT|
|Source (natural)||Organism: Gallus gallus (chicken)|
|Source (recombinant)||Organism: Homo sapiens (human)|
|Buffer solution||pH: 7.5|
|Specimen||Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES|
|Vitrification||Cryogen name: ETHANE|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Microscopy||Model: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: SPOT SCAN|
|Electron lens||Mode: BRIGHT FIELDBright-field microscopy|
|Image recording||Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k)|
|CTF correction||Type: PHASE FLIPPING AND AMPLITUDE CORRECTION|
|3D reconstruction||Resolution: 3.49 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 292613 / Symmetry type: POINT|
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