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Updated: Jun 28, 2025
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Dissection and Flat-mounting of the Threespine Stickleback Branchial Skeleton
Published on: May 7, 2016
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Mapping structural and dynamic divergence across the MBOAT family.
T Bertie Ansell1, Megan Healy2, Claire E Coupland3
1Department of Biochemistry, South Parks Road, Oxford OX1 3QU, UK; Division of CryoEM and Bioimaging, SSRL, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA; Department of Biology, Stanford University, Stanford, CA 94305, USA.
Structure (London, England : 1993)
|April 18, 2024
Summary
Membrane-bound O-acyltransferases (MBOATs) dynamically alter cell membranes based on substrate. This study reveals lipid binding sites and structural roles, aiding in designing targeted MBOAT inhibitors.
Area of Science:
- Biochemistry
- Structural Biology
- Bioinformatics
Background:
- Membrane-bound O-acyltransferases (MBOATs) are crucial enzymes with diverse functions.
- Despite a conserved core, their catalytic specificity, regulation, and environmental interactions are poorly understood.
Purpose of the Study:
- To investigate the molecular and interactional divergence within the MBOAT family.
- To elucidate the structural basis of MBOAT function and substrate specificity.
Main Methods:
- Comparative molecular dynamics (MD) simulations.
- Bioinformatic analyses.
Main Results:
- MBOATs exhibit substrate-dependent membrane distortion.
- Lipid binding sites near reactant gates were identified.
- Re-entrant loop-2 plays a conserved role in MBOAT structure and DGAT1 dimerization.
Conclusions:
- MBOATs display unique dynamic behaviors and interaction patterns.
- Understanding these dynamics is key for developing specific MBOAT inhibitors.
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