Details

Autor(en) / Beteiligte

• Zhang, Qing
• Yao, Deqiang
• Rao, Bing
• Jian, Liyan
• Chen, Yang
• Hu, Kexin
• Xia, Ying
• Li, Shaobai
• Shen, Yafeng
• Qin, An
• Zhao, Jie
• Zhou, Lu
• Lei, Ming
• Jiang, Xian-Cheng
• Cao, Yu

Titel

The structural basis for the phospholipid remodeling by lysophosphatidylcholine acyltransferase 3

Ist Teil von

• Nature communications, 2021-11, Vol.12 (1), p.6869-6869, Article 6869

Ort / Verlag

England: Nature Publishing Group

Erscheinungsjahr

2021

Link zum Volltext

Quelle

MEDLINE

Beschreibungen/Notizen

• 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.