The structure of a polyketide synthase bimodule core

Tittes, Yves U. and Herbst, Dominik A. and Martin, Solène F. X. and Munoz-Hernandez, Hugo and Jakob, Roman P. and Maier, Timm. (2022) The structure of a polyketide synthase bimodule core. Science Advances, 8 (38). eabo6918.

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Official URL: https://edoc.unibas.ch/89911/

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Polyketide synthases (PKSs) are predominantly microbial biosynthetic enzymes. They assemble highly potent bioactive natural products from simple carboxylic acid precursors. The most versatile families of PKSs are organized as assembly lines of functional modules. Each module performs one round of precursor extension and optional modification, followed by directed transfer of the intermediate to the next module. While enzymatic domains and even modules of PKSs are well understood, the higher-order modular architecture of PKS assembly lines remains elusive. Here, we visualize a PKS bimodule core using cryo-electron microscopy and resolve a two-dimensional meshwork of the bimodule core formed by homotypic interactions between modules. The sheet-like organization provides the framework for efficient substrate transfer and for sequestration of trans-acting enzymes required for polyketide production.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Maier)
UniBasel Contributors:Maier, Timm and Tittes, Yves Ulrich and Muñoz Hernández, Hugo and Jakob, Roman Peter
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:American Association for the Advancement of Science
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:03 Oct 2022 10:05
Deposited On:03 Oct 2022 10:05

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