View source for 8rpy


==Escherichia coli 50S subunit in complex with the antimicrobial peptide Api137==
<StructureSection load='8rpy' size='340' side='right'caption='[[8rpy]], [[Resolution|resolution]] 2.64&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8rpy]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8RPY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8RPY FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.64&#8491;</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=8rpy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8rpy OCA], [https://pdbe.org/8rpy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8rpy RCSB], [https://www.ebi.ac.uk/pdbsum/8rpy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8rpy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RL32_ECOLI RL32_ECOLI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Proline-rich antimicrobial peptides (PrAMPs) inhibit bacterial protein biosynthesis by binding to the polypeptide exit tunnel (PET) near the peptidyl transferase center. Api137, an optimized derivative of honeybee PrAMP apidaecin, inhibits protein expression by trapping release factors (RFs), which interact with stop codons on ribosomes to terminate translation. This study uses cryo-EM, functional assays and molecular dynamic (MD) simulations to show that Api137 additionally occupies a second binding site near the exit of the PET and can repress translation independently of RF-trapping. Api88, a C-terminally amidated (-CONH(2)) analog of Api137 (-COOH), binds to the same sites, occupies a third binding pocket and interferes with the translation process presumably without RF-trapping. In conclusion, apidaecin-derived PrAMPs inhibit bacterial ribosomes by multimodal mechanisms caused by minor structural changes and thus represent a promising pool for drug development efforts.

Multimodal binding and inhibition of bacterial ribosomes by the antimicrobial peptides Api137 and Api88.,Lauer SM, Reepmeyer M, Berendes O, Klepacki D, Gasse J, Gabrielli S, Grubmuller H, Bock LV, Krizsan A, Nikolay R, Spahn CMT, Hoffmann R Nat Commun. 2024 May 10;15(1):3945. doi: 10.1038/s41467-024-48027-4. PMID:38730238<ref>PMID:38730238</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8rpy" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Lauer S]]
[[Category: Nikolay R]]
[[Category: Spahn C]]