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Structural basis for selectivity in a highly reducing type II polyketide synthase.

Danyao Du1, Yohei Katsuyama2,3, Masanobu Horiuchi1

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|May 6, 2020
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Highly reducing polyketide synthases (PKSs) create polyenes. Structural analysis of the IgaPKS complex reveals unique ACP-KS-CLF interactions and a key residue that limits further condensation, differentiating it from typical PKSs.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Type II polyketide synthases (PKSs) are crucial for synthesizing diverse polyketide natural products.
  • Highly reducing PKSs, like IgaPKS, deviate from typical PKS pathways, producing polyenes instead of aromatic compounds.
  • Understanding the structural basis of these unique PKSs is essential for novel compound discovery and engineering.

Purpose of the Study:

  • To elucidate the structural mechanisms of the highly reducing IgaPKS, specifically the interaction between its components.
  • To identify the molecular features responsible for the unique polyene production by IgaPKS.
  • To provide insights for the rational design of novel polyketide-synthesizing enzymes.

Main Methods:

  • X-ray crystallography was employed to determine the structures of the Iga11-Iga12 (ketosynthase-chain length factor [KS-CLF]) heterodimer and the Iga10=Iga11-Iga12 (acyl carrier protein [ACP]=KS-CLF) tripartite complex.
  • Site-directed mutagenesis was used to investigate the role of specific amino acid residues in enzyme function.
  • Biochemical assays were performed to analyze enzyme activity and substrate interactions.

Main Results:

  • The crystal structure of the Iga10=Iga11-Iga12 tripartite complex revealed the molecular interactions between the ACP and KS-CLF components, highlighting differences from other fatty acid synthases.
  • Structural analysis identified a unique reaction pocket within the IgaPKS complex.
  • Mutagenesis confirmed that Asp113 in Iga11 plays a critical role by preventing further condensation of β-ketoacyl products, thereby distinguishing IgaPKS activity.

Conclusions:

  • The determined structures provide a detailed molecular understanding of the highly reducing IgaPKS.
  • The unique features of the IgaPKS reaction pocket and the role of Asp113 explain its distinct polyene-producing mechanism.
  • This research lays the foundation for engineering PKSs for the targeted synthesis of novel polyketide structures.