Biochemical and structural study of the atypical acyltransferase domain from the mycobacterial polyketide synthase Pks13.

@article{Bergeret2012BiochemicalAS,
  title={Biochemical and structural study of the atypical acyltransferase domain from the mycobacterial polyketide synthase Pks13.},
  author={Fabien Bergeret and Sabine Gavalda and Christian Chalut and Wladimir Malaga and Anna{\"i}k Qu{\'e}mard and J D P{\'e}delacq and Mamadou Daff{\'e} and Christophe Guilhot and Lionel Mourey and C{\'e}cile Bon},
  journal={The Journal of biological chemistry},
  year={2012},
  volume={287 40},
  pages={33675-90}
}
Pks13 is a type I polyketide synthase involved in the final biosynthesis step of mycolic acids, virulence factors, and essential components of the Mycobacterium tuberculosis envelope. Here, we report the biochemical and structural characterization of a 52-kDa fragment containing the acyltransferase domain of Pks13. This fragment retains the ability to load atypical extender units, unusually long chain acyl-CoA with a predilection for carboxylated substrates. High resolution crystal structures… CONTINUE READING