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The flexible linker in fusicoccadiene synthase is not essential for substrate channeling between its prenyltransferase and cyclase domains. Optimal channeling occurs when cyclase domains associate with the prenyltransferase octamer, irrespective of linkage.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Fusicoccadiene synthase (PaFS) is a bifunctional enzyme catalyzing diterpene biosynthesis.
  • It features prenyltransferase and cyclase domains linked by a flexible segment.
  • Substrate channeling is proposed to enhance catalytic efficiency.

Approach:

  • Investigated the role of the flexible linker in PaFS substrate channeling.
  • Utilized a "linkerless" PaFS construct (PaFSLL) for structural and functional analysis.
  • Employed cryo-electron microscopy (cryo-EM) to determine the structure of PaFSLL.

Key Points:

  • The flexible linker is dispensable for substrate channeling.
  • Covalent linkage between prenyltransferase and cyclase domains is not required for channeling.
  • PaFS prenyltransferase and cyclase domains exhibit preferential interaction.
  • Cryo-EM reveals cyclase pairs associate with the prenyltransferase octamer in the linkerless construct.

Conclusions:

  • Optimal substrate channeling in PaFS is achieved through the association of cyclase domains with the prenyltransferase octamer.
  • This association can be transient or stable, and does not necessitate a flexible linker.
  • Findings provide insights into the modular assembly and function of complex terpene synthases.