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

ABSTRACT: 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 were determined for the apo, palmitoylated, and carboxypalmitoylated forms. Structural conservation with type I polyketide synthases and related fatty-acid synthases also extends to the interdomain connections. Subtle changes could be identified both in the active site and in the upstream and downstre

SUBMITTER: Bergeret F 

PROVIDER: S-EPMC3460465 | biostudies-literature | 2012 Sep

REPOSITORIES: biostudies-literature