Ontology highlight
ABSTRACT:
SUBMITTER: Miyanaga A
PROVIDER: S-EPMC4763789 | biostudies-literature | 2016 Feb
REPOSITORIES: biostudies-literature
Miyanaga Akimasa A Iwasawa Shohei S Shinohara Yuji Y Kudo Fumitaka F Eguchi Tadashi T
Proceedings of the National Academy of Sciences of the United States of America 20160201 7
Acyltransferases (ATs) are key determinants of building block specificity in polyketide biosynthesis. Despite the importance of protein-protein interactions between AT and acyl carrier protein (ACP) during the acyltransfer reaction, the mechanism of ACP recognition by AT is not understood in detail. Herein, we report the crystal structure of AT VinK, which transfers a dipeptide group between two ACPs, VinL and VinP1LdACP, in vicenistatin biosynthesis. The isolated VinK structure showed a unique ...[more]