7WRP

Crystal Structure of pks13-ACP domain from Corynebacterium diphtheriae

Summary for 7WRP

• Entry DOI: 10.2210/pdb7wrp/pdb
• Descriptor: Polyketide synthase involved in mycolic acid biosynthesis, 4'-PHOSPHOPANTETHEINE (3 entities in total)
• Functional Keywords: acyl-carrier protein, recombination
• Biological source: Corynebacterium diphtheriae
• Total number of polymer chains: 1
• Total formula weight: 9707.96

Authors

Liu, X. (deposition date: 2022-01-27, release date: 2022-02-23, Last modification date: 2023-11-29)

Primary citation

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., 590:152-157, 2022

PubMed Abstract: 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.

PubMed: 34974304
DOI: 10.1016/j.bbrc.2021.12.083

Experimental method

X-RAY DIFFRACTION (1.794 Å)