Ontology highlight
ABSTRACT:
SUBMITTER: Liu C
PROVIDER: S-EPMC6127857 | biostudies-literature | 2018 Aug
REPOSITORIES: biostudies-literature
Liu Chenguang C Yuan Meijuan M Xu Xu X Wang Lei L Keatinge-Clay Adrian T AT Deng Zixin Z Lin Shuangjun S Zheng Jianting J
Journal of structural biology 20180404 2
Ketoreductase (KR) domains of modular polyketide synthases (PKSs) control the stereochemistry of C2 methyl and C3 hydroxyl substituents of polyketide intermediates. To understand the molecular basis of stereocontrol exerted by KRs, the crystal structure of a KR from the second module of the amphotericin PKS (AmpKR2) complexed with NADP<sup>+</sup> and 2-methyl-3-oxopentanoyl-pantetheine was solved. This first ternary structure provides direct evidence to the hypothesis that a substrate enters in ...[more]