Unknown

Dataset Information

0

Structure and mechanism of assembly line polyketide synthases.


ABSTRACT: Assembly line polyketide synthases (PKSs) are remarkable biosynthetic machines with considerable potential for structure-based engineering. Several types of protein-protein interactions, both within and between PKS modules, play important roles in the catalytic cycle of a multimodular PKS. Additionally, vectorial biosynthesis is enabled by the energetic coupling of polyketide chain elongation to the channeling of intermediates between successive modules. A combination of high-resolution analysis of smaller PKS components and lower resolution characterization of intact modules and bimodules has yielded insights into the structure and organization of a prototypical assembly line PKS. This review discusses our understanding of key structure-function relationships in this family of megasynthases, along with a recap of key unanswered questions in the field.

SUBMITTER: Robbins T 

PROVIDER: S-EPMC5136517 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature

altmetric image

Publications

Structure and mechanism of assembly line polyketide synthases.

Robbins Thomas T   Liu Yu-Chen YC   Cane David E DE   Khosla Chaitan C  

Current opinion in structural biology 20160605


Assembly line polyketide synthases (PKSs) are remarkable biosynthetic machines with considerable potential for structure-based engineering. Several types of protein-protein interactions, both within and between PKS modules, play important roles in the catalytic cycle of a multimodular PKS. Additionally, vectorial biosynthesis is enabled by the energetic coupling of polyketide chain elongation to the channeling of intermediates between successive modules. A combination of high-resolution analysis  ...[more]

Similar Datasets

| S-EPMC10394414 | biostudies-literature
| S-EPMC4020578 | biostudies-other
| S-EPMC4731828 | biostudies-literature
| S-EPMC3971720 | biostudies-literature
| S-EPMC4028714 | biostudies-literature
| S-EPMC4963262 | biostudies-literature
| S-EPMC8256042 | biostudies-literature
| S-EPMC4965586 | biostudies-literature
| S-EPMC4067149 | biostudies-literature
| S-EPMC8683866 | biostudies-literature