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A look into DGAT1 through the EM lenses
Rashmi Panigrahi1, J N Mark Glover1, Saranya Nallusamy2
1Department of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2H7, Canada.
Biochimica Et Biophysica Acta. Biomembranes
|October 10, 2022
Summary
Cryo-electron microscopy revealed new insights into DGAT1, an enzyme crucial for triglyceride synthesis. Structural data explains its preference for long fatty acyl chains and the mechanism of histidine flipping during catalysis.
Area of Science:
- Structural biology
- Biochemistry
- Membrane protein research
Background:
- Membrane proteins, like DGAT1, are vital but difficult to study structurally.
- DGAT1 is a key enzyme in triglyceride synthesis, with extensive research on its activity.
- Cryo-electron microscopy (cryo-EM) has advanced structural biology capabilities.
Purpose of the Study:
- To review recent cryo-EM structures of DGAT1.
- To provide mechanistic insights into DGAT1 function.
- To explain DGAT1's substrate preference and catalytic mechanism.
Main Methods:
- Cryo-electron microscopy (cryo-EM) for structure determination.
- Analysis of apo and ligand-bound DGAT1 structures.
- Comparative analysis of enzyme structures and biochemical data.
Main Results:
- Recent cryo-EM structures of DGAT1 (apo and bound forms) offer critical mechanistic insights.
- The flipping of a catalytic histidine residue is essential for enzyme catalysis.
- Structural data elucidates DGAT1's preference for long over short fatty acyl chains.
Conclusions:
- Cryo-EM has revolutionized the study of challenging targets like DGAT1.
- The solved structures provide a molecular basis for DGAT1's substrate specificity.
- Understanding DGAT1's mechanism is key for metabolic research and drug development.
