Structural highlights
Function
Q6NES8_CORDI
Publication Abstract from PubMed
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.
Crystal structures of FadD32 and pks13-ACP domain from Corynebacterium diphtheriae.,Chen R, Yuan J, Shi X, Tang W, Liu X Biochem Biophys Res Commun. 2022 Jan 29;590:152-157. doi:, 10.1016/j.bbrc.2021.12.083. Epub 2021 Dec 25. PMID:34974304[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chen R, Yuan J, Shi X, Tang W, Liu X. Crystal structures of FadD32 and pks13-ACP domain from Corynebacterium diphtheriae. Biochem Biophys Res Commun. 2022 Jan 29;590:152-157. PMID:34974304 doi:10.1016/j.bbrc.2021.12.083
