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Structure-Function Analysis of the Extended Conformation of a Polyketide Synthase Module.

Xiuyuan Li, Natalia Sevillano1, Florencia La Greca1

  • 1Department of Pharmaceutical Chemistry , University of California San Francisco , San Francisco , California 94158 , United States.

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|May 16, 2018
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Researchers identified a specific structure, the extended conformation, of polyketide synthases (PKS) that is fully capable of catalyzing essential enzymatic reactions. This finding clarifies the functional role of PKS module architectures in polyketide biosynthesis.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Assembly-line polyketide synthases (PKS) are large multi-enzyme complexes.
  • PKS modules have been observed in distinct conformations, including 'extended' and 'arch-shaped' architectures.
  • The catalytic relevance of these different PKS conformations remained unestablished.

Purpose of the Study:

  • To determine the catalytic competence of the extended conformation of a PKS module.
  • To investigate the functional significance of PKS module architecture.

Main Methods:

  • Utilized a fully human naïve antigen-binding fragment (Fab) library to isolate a high-affinity antibody targeting the extended PKS conformation.
  • Verified the antibody-bound conformation using X-ray crystallography and SEC-SAXS.
  • Performed kinetic analyses to assess catalytic activity.

Main Results:

  • A high-affinity antibody specifically bound to the extended conformation of a PKS module.
  • Structural analyses confirmed the antibody-stabilized extended conformation.
  • Kinetic studies demonstrated that this conformation is fully competent for intermodular chain translocation, intramodular chain elongation, and functional group modification.

Conclusions:

  • The extended conformation of a PKS module is catalytically active and competent for all its essential enzymatic functions.
  • This study establishes the functional relevance of the extended PKS module architecture in polyketide biosynthesis.