5O2R

Cryo-EM structure of the proline-rich antimicrobial peptide Api137 bound to the terminating ribosome

This is a non-PDB format compatible entry.

Summary for 5O2R

• Entry DOI: 10.2210/pdb5o2r/pdb
• EMDB information: 3730
• Descriptor: 23S ribosomal RNA, 50S ribosomal protein L13, 50S ribosomal protein L14, ... (58 entities in total)
• Functional Keywords: ribosome, termination, release factors, antimicrobial peptides, antibiotic
• Biological source: Escherichia coli K-12; More
• Total number of polymer chains: 58
• Total formula weight: 2196433.95

Authors

Graf, M.,Berninghausen, O.,Beckmann, R.,Wilson, D.N. (deposition date: 2017-05-22, release date: 2017-07-26, Last modification date: 2019-02-20)

Primary citation

Florin, T.,Maracci, C.,Graf, M.,Karki, P.,Klepacki, D.,Berninghausen, O.,Beckmann, R.,Vazquez-Laslop, N.,Wilson, D.N.,Rodnina, M.V.,Mankin, A.S.
An antimicrobial peptide that inhibits translation by trapping release factors on the ribosome.
Nat. Struct. Mol. Biol., 24:752-757, 2017

PubMed Abstract: Many antibiotics stop bacterial growth by inhibiting different steps of protein synthesis. However, no specific inhibitors of translation termination are known. Proline-rich antimicrobial peptides, a component of the antibacterial defense system of multicellular organisms, interfere with bacterial growth by inhibiting translation. Here we show that Api137, a derivative of the insect-produced antimicrobial peptide apidaecin, arrests terminating ribosomes using a unique mechanism of action. Api137 binds to the Escherichia coli ribosome and traps release factor (RF) RF1 or RF2 subsequent to the release of the nascent polypeptide chain. A high-resolution cryo-EM structure of the ribosome complexed with RF1 and Api137 reveals the molecular interactions that lead to RF trapping. Api137-mediated depletion of the cellular pool of free release factors causes the majority of ribosomes to stall at stop codons before polypeptide release, thereby resulting in a global shutdown of translation termination.

PubMed: 28741611
DOI: 10.1038/nsmb.3439

Experimental method

ELECTRON MICROSCOPY (3.4 Å)