8ana

Cryo-EM structure of the proline-rich antimicrobial peptide drosocin bound to the 50S ribosomal subunit

spinqualitylabelsall models 8ana, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8ana is a 10 chain structure with sequence from Escherichia coli BW25113. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.1Å Ligands: 1MG, 2MA, 2MG, 5MC, 5MU, A2G, G7M, H2U, MEQ, MG, OMC, OMG, OMU, PSU, SPM, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RL13_ECOLI This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.[HAMAP-Rule:MF_01366] Publication Abstract from PubMed 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-A 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. Structural basis for translation inhibition by the glycosylated drosocin peptide.,Koller TO, Morici M, Berger M, Safdari HA, Lele DS, Beckert B, Kaur KJ, Wilson DN Nat Chem Biol. 2023 Sep;19(9):1072-1081. doi: 10.1038/s41589-023-01293-7. Epub , 2023 Mar 30. PMID:36997646 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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