The structural basis for the phospholipid remodeling by lysophosphatidylcholine acyltransferase 3

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 and Yu Cao ()
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Qing Zhang: Chinese Academy of Sciences, University of Chinese Academy of Sciences
Deqiang Yao: Shanghai Jiao Tong University School of Medicine
Bing Rao: Shanghai Jiao Tong University School of Medicine
Liyan Jian: Shanghai Jiao Tong University School of Medicine
Yang Chen: Shanghai Jiao Tong University School of Medicine
Kexin Hu: Shanghai Jiao Tong University School of Medicine
Ying Xia: Shanghai Jiao Tong University School of Medicine
Shaobai Li: Shanghai Jiao Tong University School of Medicine
Yafeng Shen: Shanghai Jiao Tong University School of Medicine
An Qin: Shanghai Jiao Tong University School of Medicine
Jie Zhao: Shanghai Jiao Tong University School of Medicine
Lu Zhou: Fudan University
Ming Lei: Shanghai Jiao Tong University School of Medicine
Xian-Cheng Jiang: State University of New York Downstate Health Sciences University
Yu Cao: Shanghai Jiao Tong University School of Medicine

Nature Communications, 2021, vol. 12, issue 1, 1-11

Abstract: 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 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.

Date: 2021
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DOI: 10.1038/s41467-021-27244-1

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