|Title||The structural basis for the phospholipid remodeling by lysophosphatidylcholine acyltransferase 3.|
|Journal, issue, pages||Nat Commun, Vol. 12, Issue 1, Page 6869, Year 2021|
|Publish date||Nov 25, 2021|
|Authors||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 /|
|PubMed 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 ...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 links||Nat Commun / PubMed:34824256 / PubMed Central|
|Methods||EM (single particle) / X-ray diffraction|
|Resolution||3.4 - 3.57 Å|
|Keywords||TRANSFERASE / Lysophospholipid Acyltransferase / membrane bound O-acyltransferase / phospholipid remodeling / MEMBRANE PROTEIN / LPCAT3 / membrane-bound O-acyltransferase / cryo-EM|
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