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Structure paper

TitleStructural basis for translation inhibition by the glycosylated drosocin peptide.
Journal, issue, pagesNat Chem Biol, Vol. 19, Issue 9, Page 1072-1081, Year 2023
Publish dateMar 30, 2023
AuthorsTimm O Koller / Martino Morici / Max Berger / Haaris A Safdari / Deepti S Lele / Bertrand Beckert / Kanwal J Kaur / Daniel N Wilson /
PubMed AbstractThe 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- ...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 at 2.0-2.8-Å resolution reveal that the peptide interferes with translation termination by binding within the polypeptide exit tunnel and trapping RF1 on the ribosome, reminiscent of that reported for the PrAMP apidaecin. The glycosylation of drosocin enables multiple interactions with U2609 of the 23S rRNA, leading to conformational changes that break the canonical base pair with A752. Collectively, our study reveals novel molecular insights into the interaction of O-glycosylated drosocin with the ribosome, which provide a structural basis for future development of this class of antimicrobials.
External linksNat Chem Biol / PubMed:36997646 / PubMed Central
MethodsEM (single particle)
Resolution2.1 - 2.8 Å
Structure data

15488

8akn

EMDB-15488, PDB-8akn:
Cryo-EM structure of the proline-rich antimicrobial peptide drosocin bound to the terminating ribosome
Method: EM (single particle) / Resolution: 2.3 Å

15523

8am9

EMDB-15523, PDB-8am9:
Cryo-EM structure of the proline-rich antimicrobial peptide drosocin bound to the elongating ribosome
Method: EM (single particle) / Resolution: 2.8 Å

15533

8ana

EMDB-15533, PDB-8ana:
Cryo-EM structure of the proline-rich antimicrobial peptide drosocin bound to the 50S ribosomal subunit
Method: EM (single particle) / Resolution: 2.1 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-A2G:
2-acetamido-2-deoxy-alpha-D-galactopyranose

ChemComp-MG:
Unknown entry

ChemComp-SPM:
SPERMINE

ChemComp-HOH:
WATER

Source
  • escherichia coli bw25113 (bacteria)
  • drosophila melanogaster (fruit fly)
  • Escherichia coli K-12 (bacteria)
KeywordsRIBOSOME / E.coli / 70S / Drosocin / Dro1 / antimicrobial peptide / proline-rich / PrAMP / Release factor 1 / RF1 / Initiator tRNA / Elongation / Leucine tRNA / 50S

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