The structural basis for the phospholipid remodeling by lysophosphatidylcholine acyltransferase 3

During phosphatidylcholine (PC) remodeling re-acylation is catalyzed by lysophosphatidylcholine acyltransferases (LPCAT). Here, the authors present crystal and cryo-EM structures of chicken LPCAT3 in the apo-, acyl donor-bound and acyl receptor-bound states, and based on the structures and further f...

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Autores principales:	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
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/6de1b72018e541e28fd5d13bfcea2813
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spelling	oai:doaj.org-article:6de1b72018e541e28fd5d13bfcea28132021-11-28T12:33:19ZThe structural basis for the phospholipid remodeling by lysophosphatidylcholine acyltransferase 310.1038/s41467-021-27244-12041-1723https://doaj.org/article/6de1b72018e541e28fd5d13bfcea28132021-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-27244-1https://doaj.org/toc/2041-1723During phosphatidylcholine (PC) remodeling re-acylation is catalyzed by lysophosphatidylcholine acyltransferases (LPCAT). Here, the authors present crystal and cryo-EM structures of chicken LPCAT3 in the apo-, acyl donor-bound and acyl receptor-bound states, and based on the structures and further functional analysis they discuss the mechanism of the enzyme.Qing ZhangDeqiang YaoBing RaoLiyan JianYang ChenKexin HuYing XiaShaobai LiYafeng ShenAn QinJie ZhaoLu ZhouMing LeiXian-Cheng JiangYu CaoNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q 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 The structural basis for the phospholipid remodeling by lysophosphatidylcholine acyltransferase 3
description	During phosphatidylcholine (PC) remodeling re-acylation is catalyzed by lysophosphatidylcholine acyltransferases (LPCAT). Here, the authors present crystal and cryo-EM structures of chicken LPCAT3 in the apo-, acyl donor-bound and acyl receptor-bound states, and based on the structures and further functional analysis they discuss the mechanism of the enzyme.
format	article
author	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
author_facet	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
author_sort	Qing Zhang
title	The structural basis for the phospholipid remodeling by lysophosphatidylcholine acyltransferase 3
title_short	The structural basis for the phospholipid remodeling by lysophosphatidylcholine acyltransferase 3
title_full	The structural basis for the phospholipid remodeling by lysophosphatidylcholine acyltransferase 3
title_fullStr	The structural basis for the phospholipid remodeling by lysophosphatidylcholine acyltransferase 3
title_full_unstemmed	The structural basis for the phospholipid remodeling by lysophosphatidylcholine acyltransferase 3
title_sort	structural basis for the phospholipid remodeling by lysophosphatidylcholine acyltransferase 3
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/6de1b72018e541e28fd5d13bfcea2813
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The structural basis for the phospholipid remodeling by lysophosphatidylcholine acyltransferase 3

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