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TitleThe structure of phosphatidylinositol remodeling MBOAT7 reveals its catalytic mechanism and enables inhibitor identification.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 3533, Year 2023
Publish dateJun 14, 2023
AuthorsKun Wang / Chia-Wei Lee / Xuewu Sui / Siyoung Kim / Shuhui Wang / Aidan B Higgs / Aaron J Baublis / Gregory A Voth / Maofu Liao / Tobias C Walther / Robert V Farese /
PubMed AbstractCells remodel glycerophospholipid acyl chains via the Lands cycle to adjust membrane properties. Membrane-bound O-acyltransferase (MBOAT) 7 acylates lyso-phosphatidylinositol (lyso-PI) with ...Cells remodel glycerophospholipid acyl chains via the Lands cycle to adjust membrane properties. Membrane-bound O-acyltransferase (MBOAT) 7 acylates lyso-phosphatidylinositol (lyso-PI) with arachidonyl-CoA. MBOAT7 mutations cause brain developmental disorders, and reduced expression is linked to fatty liver disease. In contrast, increased MBOAT7 expression is linked to hepatocellular and renal cancers. The mechanistic basis of MBOAT7 catalysis and substrate selectivity are unknown. Here, we report the structure and a model for the catalytic mechanism of human MBOAT7. Arachidonyl-CoA and lyso-PI access the catalytic center through a twisted tunnel from the cytosol and lumenal sides, respectively. N-terminal residues on the ER lumenal side determine phospholipid headgroup selectivity: swapping them between MBOATs 1, 5, and 7 converts enzyme specificity for different lyso-phospholipids. Finally, the MBOAT7 structure and virtual screening enabled identification of small-molecule inhibitors that may serve as lead compounds for pharmacologic development.
External linksNat Commun / PubMed:37316513 / PubMed Central
MethodsEM (single particle)
Resolution3.7 Å
Structure data

28552

8erc

EMDB-28552, PDB-8erc:
Human Membrane-bound O-acyltransferase 7
Method: EM (single particle) / Resolution: 3.7 Å

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / lipid metabolism membrane remodeling

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