8am9

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Current revision (09:26, 17 October 2024) (edit) (undo)
 
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8am9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8am9 OCA], [https://pdbe.org/8am9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8am9 RCSB], [https://www.ebi.ac.uk/pdbsum/8am9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8am9 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8am9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8am9 OCA], [https://pdbe.org/8am9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8am9 RCSB], [https://www.ebi.ac.uk/pdbsum/8am9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8am9 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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<div style="background-color:#fffaf0;">
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[https://www.uniprot.org/uniprot/D8A1N0_ECOMS D8A1N0_ECOMS] Forms part of the polypeptide exit tunnel.[HAMAP-Rule:MF_01328] One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.[HAMAP-Rule:MF_01328]
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== Publication Abstract from PubMed ==
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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.
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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<ref>PMID:36997646</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 8am9" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Ribosome 3D structures|Ribosome 3D structures]]
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== References ==
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<references/>
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</StructureSection>
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Current revision

Cryo-EM structure of the proline-rich antimicrobial peptide drosocin bound to the elongating ribosome

PDB ID 8am9

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