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The structure of a polyketide synthase bimodule core
Yves U Tittes1, Dominik A Herbst1, Solène F X Martin1
1Biozentrum, University of Basel, Spitalstrasse 41, Basel 4056, Switzerland.
Science Advances
|September 21, 2022
Summary
Polyketide synthases (PKSs) are microbial enzymes. Cryo-EM reveals a novel 2D meshwork of PKS modules, explaining efficient substrate transfer and enzyme sequestration for natural product biosynthesis.
Area of Science:
- Biochemistry
- Molecular Biology
- Structural Biology
Background:
- Polyketide synthases (PKSs) are crucial microbial enzymes that synthesize complex natural products.
- PKSs function as modular assembly lines, with each module catalyzing specific reactions.
- The higher-order organization of these modular assembly lines is not well understood.
Purpose of the Study:
- To elucidate the structural organization of the polyketide synthase (PKS) bimodule core.
- To understand the higher-order architecture of PKS assembly lines.
Main Methods:
- Cryo-electron microscopy (cryo-EM) was used to visualize the PKS bimodule core.
- Structural analysis was performed to resolve the arrangement of modules.
Main Results:
- A two-dimensional meshwork structure of the PKS bimodule core was resolved.
- This sheet-like organization arises from homotypic interactions between modules.
- The observed structure facilitates efficient substrate transfer and sequestration of necessary trans-acting enzymes.
Conclusions:
- The study reveals a novel higher-order organization of PKS assembly lines.
- This structural framework is essential for the efficient production of polyketides.
- Understanding PKS architecture provides insights into natural product biosynthesis.
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