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Structural and Functional Insights into an Archaeal Lipid Synthase
Sixue Ren1, Niels A W de Kok2, Yijun Gu3
1Division of Respiratory and Critical Care Medicine, Respiratory Infection and Intervention Laboratory of Frontiers Science Center for Disease-Related Molecular Network, State Key Laboratory of Biotherapy, West China Hospital of Sichuan University, Chengdu 610041, China.
Cell Reports
|October 21, 2020
Summary
Digeranylgeranylglyceryl phosphate synthase (DGGGPase) is a key enzyme in archaeal lipid biosynthesis. Its crystal structure reveals a unique mechanism for binding hydrophobic substrates, offering insights into membrane lipid remodeling.
Area of Science:
- Biochemistry
- Structural Biology
- Membrane Biology
Background:
- The UbiA superfamily comprises intramembrane prenyltransferases crucial for lipophilic compound biosynthesis.
- Digeranylgeranylglyceryl phosphate synthase (DGGGPase) synthesizes unique membrane core lipids in archaea, essential for ether bond formation.
Purpose of the Study:
- To elucidate the structural basis of DGGGPase function within the UbiA superfamily.
- To understand the mechanism of hydrophobic substrate binding and lipid biosynthesis in archaea.
Main Methods:
- X-ray crystallography to determine the three-dimensional structure of DGGGPase.
- Analysis of lipid-bound enzyme states to infer substrate interaction modes.
Main Results:
- The crystal structure reveals DGGGPase possesses nine transmembrane helices, a cytosolic cap domain, and a central substrate-binding cavity.
- Lipid-bound states indicate the enzyme's pocket accommodates hydrophobic substrates during crystallization.
- Structural insights into the unique membrane core lipid biosynthesis pathway.
Conclusions:
- DGGGPase structure provides a mechanistic understanding of lipid biosynthesis by specific lipid-modifying enzymes.
- The findings offer insights into lipid membrane remodeling and adaptation strategies in archaea.
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