Ontology highlight
ABSTRACT:
SUBMITTER: Braffman NR
PROVIDER: S-EPMC6347699 | biostudies-literature | 2019 Jan
REPOSITORIES: biostudies-literature
Braffman Nathaniel R NR Piscotta Frank J FJ Hauver Jesse J Campbell Elizabeth A EA Link A James AJ Darst Seth A SA
Proceedings of the National Academy of Sciences of the United States of America 20190109 4
We report crystal structures of the antibacterial lasso peptides microcin J25 (MccJ25) and capistruin (Cap) bound to their natural enzymatic target, the bacterial RNA polymerase (RNAP). Both peptides bind within the RNAP secondary channel, through which NTP substrates enter the RNAP active site, and sterically block trigger-loop folding, which is essential for efficient catalysis by the RNAP. MccJ25 binds deep within the secondary channel in a manner expected to interfere with NTP substrate bind ...[more]