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Crystal structures of FadD32 and pks13-ACP domain from Corynebacterium diphtheriae

Rong Chen1, Jingting Yuan1, Xiaoqian Shi1

  • 1State Key Laboratory of Medicinal Chemical Biology, Frontiers Science Center for Cell Responses, College of Life Sciences, Nankai University, 300071, Tianjin, China.

Biochemical and Biophysical Research Communications
|January 2, 2022
PubMed

Insights

Researchers elucidated the structures of key proteins involved in mycolic acid synthesis, a crucial factor in Mycobacterium and Corynebacterium virulence. These findings offer insights into novel anti-tuberculosis drug development.

Area of Science:

  • Microbiology
  • Structural Biology
  • Drug Discovery

Background:

  • Mycolic acids (MAs) are essential virulence factors in Mycobacterium and Corynebacterium species.
  • MA biosynthesis is a promising target for developing new anti-tuberculosis (TB) drugs.

Purpose of the Study:

  • To investigate the structures and functions of proteins in the MA biosynthesis pathway.
  • To provide structural insights into the assembly of FadD32 and polyketide synthase 13 (pks13).

Main Methods:

  • X-ray crystallography was used to determine the structures of FadD32 with substrates.
  • The holo-form of the ACP-domain from Corynebacterium diphtheriae was also crystallized.
  • In vitro biochemical assays were performed to analyze protein function.

Main Results:

  • Crystal structures of FadD32 bound to substrates were obtained.
  • The holo-form structure of the ACP-domain from C. diphtheriae was determined.
  • Structural and biochemical data revealed new insights into the assembly of FadD32 and pks13.

Conclusions:

  • The elucidated structures provide a foundation for understanding the MA biosynthesis mechanism.
  • These findings could guide the rational design of novel anti-TB agents targeting FadD32 and pks13.
Keywords:
Corynebacterium diphtheriaeFadD32Mycobacterium tuberculosisMycolic acid biosynthesispks13

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