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

Mycolic acids (MAs) are unique components of cell envelope of Mycobacterium or Corynebacterium and are key factors of their virulence to human. In order to develop new anti-Tuberculosis (TB) drugs, many efforts have paid on investigation of structures and functions of proteins involved in the biosyn...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2022-01, Vol.590, p.152-157
Main Authors: Chen, Rong, Yuan, Jingting, Shi, Xiaoqian, Tang, Wenjian, Liu, Xiang
Format: Article
Language:English
Subjects:
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
Corynebacterium diphtheriae
Corynebacterium diphtheriae - metabolism
Crystallography, X-Ray
FadD32
Ligands
Models, Molecular
Mycobacterium tuberculosis
Mycolic acid biosynthesis
pks13
Protein Binding
Protein Domains
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Summary:Mycolic acids (MAs) are unique components of cell envelope of Mycobacterium or Corynebacterium and are key factors of their virulence to human. In order to develop new anti-Tuberculosis (TB) drugs, many efforts have paid on investigation of structures and functions of proteins involved in the biosynthesis pathway of MAs. FadD32 and polyketide synthase 13 (pks13) catalyze the last step of MAs synthesis. Here we present the crystal structures of FadD32 with substrates and holo-form of ACP-domain from Corynebacterium diphtheriae. The crystal structures and in vitro biochemical assays provide new insights into the assembly of FadD32 and pks13. •Mycolic acids are unique components of cell envelope of Mycobacterium or Corynebacterium.•FadD32 and polyketide synthase 13, which catalyze the last step of Mycolic acids synthesis are essential drug targets.•Crystal structures and in vitro biochemical assays provide new insights into the assembly of FadD32 and pks13.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2021.12.083