7EWT
The crystal structure of Lysophospholipid acyltransferase LPCAT3 (MOBAT5) in its monomeric and apo form
7EWT の概要
| エントリーDOI | 10.2210/pdb7ewt/pdb |
| 分子名称 | Lysophospholipid acyltransferase 5 (1 entity in total) |
| 機能のキーワード | lysophospholipid acyltransferase, membrane bound o-acyltransferase, phospholipid remodeling, membrane protein, transferase |
| 由来する生物種 | Gallus gallus (Chicken) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 51881.89 |
| 構造登録者 | |
| 主引用文献 | Zhang, Q.,Yao, D.,Rao, B.,Jian, L.,Chen, Y.,Hu, K.,Xia, Y.,Li, S.,Shen, Y.,Qin, A.,Zhao, J.,Zhou, L.,Lei, M.,Jiang, X.C.,Cao, Y. The structural basis for the phospholipid remodeling by lysophosphatidylcholine acyltransferase 3. Nat Commun, 12:6869-6869, 2021 Cited by 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 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. PubMed: 34824256DOI: 10.1038/s41467-021-27244-1 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.4 Å) |
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