Cryo-Electron microscopy of the antimicrobial peptide Drosocin from Drosophila melanogaster bound to the E.coli 70S ribosome.
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ABSTRACT:
SUBMITTER: Timm Oliver Koller
PROVIDER: EMPIAR-11388 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Structural basis for translation inhibition by the glycosylated drosocin peptide.
Koller Timm O TO Morici Martino M Berger Max M Safdari Haaris A HA Lele Deepti S DS Beckert Bertrand B Kaur Kanwal J KJ Wilson Daniel N DN
Nature chemical biology 20230330 9
The proline-rich antimicrobial peptide (PrAMP) drosocin is produced by Drosophila species to combat bacterial infection. Unlike many PrAMPs, drosocin is O-glycosylated at threonine 11, a post-translation modification that enhances its antimicrobial activity. Here we demonstrate that the O-glycosylation not only influences cellular uptake of the peptide but also interacts with its intracellular target, the ribosome. Cryogenic electron microscopy structures of glycosylated drosocin on the ribosome ...[more]
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