7KIL

Crystal structure of the mouse lipin-1 M-Lip domain with zinc

7KIL の概要

• エントリーDOI: 10.2210/pdb7kil/pdb
• 関連するPDBエントリー: 7KIH
• 分子名称: Isoform 2 of Phosphatidate phosphatase LPIN1, ZINC ION, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: lipin, m-lip, dimer, lipid binding protein
• 由来する生物種: Mus musculus (Mouse)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 21116.48

構造登録者

Gu, W.,Airola, M.V. (登録日: 2020-10-23, 公開日: 2021-07-07, 最終更新日: 2023-10-18)

主引用文献

Gu, W.,Gao, S.,Wang, H.,Fleming, K.D.,Hoffmann, R.M.,Yang, J.W.,Patel, N.M.,Choi, Y.M.,Burke, J.E.,Reue, K.,Airola, M.V.
The middle lipin domain adopts a membrane-binding dimeric protein fold.
Nat Commun, 12:4718-4718, 2021

PubMed Abstract: Phospholipid synthesis and fat storage as triglycerides are regulated by lipin phosphatidic acid phosphatases (PAPs), whose enzymatic PAP function requires association with cellular membranes. Using hydrogen deuterium exchange mass spectrometry, we find mouse lipin 1 binds membranes through an N-terminal amphipathic helix, the Ig-like domain and HAD phosphatase catalytic core, and a middle lipin (M-Lip) domain that is conserved in mammalian and mammalian-like lipins. Crystal structures of the M-Lip domain reveal a previously unrecognized protein fold that dimerizes. The isolated M-Lip domain binds membranes both in vitro and in cells through conserved basic and hydrophobic residues. Deletion of the M-Lip domain in lipin 1 reduces PAP activity, membrane association, and oligomerization, alters subcellular localization, diminishes acceleration of adipocyte differentiation, but does not affect transcriptional co-activation. This establishes the M-Lip domain as a dimeric protein fold that binds membranes and is critical for full functionality of mammalian lipins.

PubMed: 34354069
DOI: 10.1038/s41467-021-24929-5

実験手法

X-RAY DIFFRACTION (1.898 Å)