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Visualizing acyl carrier protein interactions within a crosslinked type I polyketide synthase.

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We revealed the structure of mycocerosic acid synthase from Mycobacterium tuberculosis, showing how it builds complex molecules through an iterative cycle. These findings offer new targets for tuberculosis drug development.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Microbiology

Background:

  • Mycocerosic acids are essential components of the Mycobacterium tuberculosis cell wall.
  • Mycocerosic acid synthase (MAS) is a key enzyme in the biosynthesis of these mycocerosic acids.
  • Understanding MAS structure and function is crucial for developing new anti-tuberculosis therapies.

Purpose of the Study:

  • To elucidate the structure of mycocerosic acid synthase from Mycobacterium tuberculosis.
  • To understand the enzyme's catalytic mechanism during iterative polyketide biosynthesis.
  • To identify potential targets for therapeutic intervention.

Main Methods:

  • Dual covalent crosslinking techniques were employed to stabilize distinct catalytic states of MAS.
  • Cryo-electron microscopy (cryo-EM) was used to determine the high-resolution structures.
  • Analysis of crosslinked species provided insights into domain interactions and substrate positioning.

Main Results:

  • The study resolved structures of MAS in two distinct catalytic states.
  • Dual site-selective crosslinking revealed the domain architecture of the acyl carrier protein (ACP) and its interaction with ketosynthase and dehydratase domains.
  • Key interactions and the enzyme's twisting and tilting architecture facilitating iterative substrate processing were elucidated.

Conclusions:

  • The determined structures provide unprecedented detail into the iterative vectorial polyketide biosynthesis mechanism of MAS.
  • These insights are valuable for the rational design of novel therapeutics targeting mycocerosic acid biosynthesis in Mycobacterium tuberculosis.
  • The study highlights the importance of structural biology in understanding essential microbial pathways.