Ontology highlight
ABSTRACT:
SUBMITTER: Keatinge-Clay A
PROVIDER: S-EPMC3496180 | biostudies-literature | 2008 Dec
REPOSITORIES: biostudies-literature
Journal of molecular biology 20081011 4
The dehydratases (DHs) of modular polyketide synthases (PKSs) catalyze dehydrations that occur frequently in the biosynthesis of complex polyketides, yet little is known about them structurally or mechanistically. Here, the structure of a DH domain, isolated from the fourth module of the erythromycin PKS, is presented at 1.85 A resolution. As with the DH of the highly related animalian fatty acid synthase, the DH monomer possesses a double-hotdog fold. Two symmetry mates within the crystal latti ...[more]