Structural and bioinformatic characterization of an Acinetobacter baumannii type II carrier protein.

ABSTRACT: Microorganisms produce a variety of natural products via secondary metabolic biosynthetic pathways. Two of these types of synthetic systems, the nonribosomal peptide synthetases (NRPSs) and polyketide synthases (PKSs), use large modular enzymes containing multiple catalytic domains in a single protein. These multidomain enzymes use an integrated carrier protein domain to transport the growing, covalently bound natural product to the neighboring catalytic domains for each step in the synthesis. Interestingly, some PKS and NRPS clusters contain free-standing domains that interact intermolecularly with other proteins. Being expressed outside the architecture of a multi-domain protein, these so-called type II proteins present challenges to understand the precise role they play. Additional stru

SUBMITTER: Allen CL 

PROVIDER: S-EPMC4051507 | biostudies-literature | 2014 Jun

REPOSITORIES: biostudies-literature