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TitleThe structural basis for the phospholipid remodeling by lysophosphatidylcholine acyltransferase 3.
Journal, issue, pagesNat Commun, Vol. 12, Issue 1, Page 6869, Year 2021
Publish dateNov 25, 2021
AuthorsQing 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 /
PubMed AbstractAs 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.
External linksNat Commun / PubMed:34824256 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution3.4 - 3.57 Å
Structure data

EMDB-31442, PDB-7f3x:
Lysophospholipid acyltransferase LPCAT3 in complex with lysophosphatidylcholine
Method: EM (single particle) / Resolution: 3.57 Å

EMDB-31443, PDB-7f40:
Lysophospholipid acyltransferase LPCAT3 in a complex with Arachidonoyl-CoA
Method: EM (single particle) / Resolution: 3.49 Å

PDB-7ewt:
The crystal structure of Lysophospholipid acyltransferase LPCAT3 (MOBAT5) in its monomeric and apo form
Method: X-RAY DIFFRACTION / Resolution: 3.4 Å

Chemicals

ChemComp-LAP:
[2-((1-OXODODECANOXY-(2-HYDROXY-3-PROPANYL))-PHOSPHONATE-OXY)-ETHYL]-TRIMETHYLAMMONIUM

ChemComp-3IX:
S-[2-[3-[[(2R)-4-[[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-3,3-dimethyl-2-oxidanyl-butanoyl]amino]propanoylamino]ethyl] (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenethioate

ChemComp-PCW:
1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE / DOPC, phospholipid*YM

Source
  • gallus gallus (chicken)
KeywordsTRANSFERASE / Lysophospholipid Acyltransferase / membrane bound O-acyltransferase / phospholipid remodeling / MEMBRANE PROTEIN / LPCAT3 / membrane-bound O-acyltransferase / cryo-EM

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