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Structure paper

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

31442

7f3x

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

31443

7f40

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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