6FKR

Crystal structure of the dolphin proline-rich antimicrobial peptide Tur1A bound to the Thermus thermophilus 70S ribosome

This is a non-PDB format compatible entry.

Summary for 6FKR

• Entry DOI: 10.2210/pdb6fkr/pdb
• Descriptor: 23S ribosomal RNA, 50S ribosomal protein L14, 50S ribosomal protein L15, ... (58 entities in total)
• Functional Keywords: antimicrobial peptide, antibiotic, inhibitor, ribosome
• Biological source: Escherichia coli (strain K12); More
• Total number of polymer chains: 107
• Total formula weight: 4356763.81

Authors

Mardirossian, M.,Perebaskine, N.,Benincasa, M.,Gambato, S.,Hofmann, S.,Huter, P.,Muller, C.,Hilpert, K.,Innis, C.A.,Tossi, A.,Wilson, D.N. (deposition date: 2018-01-24, release date: 2018-03-28, Last modification date: 2024-04-24)

Primary citation

Mardirossian, M.,Perebaskine, N.,Benincasa, M.,Gambato, S.,Hofmann, S.,Huter, P.,Muller, C.,Hilpert, K.,Innis, C.A.,Tossi, A.,Wilson, D.N.
The Dolphin Proline-Rich Antimicrobial Peptide Tur1A Inhibits Protein Synthesis by Targeting the Bacterial Ribosome.
Cell Chem Biol, 25:530-539.e7, 2018

PubMed Abstract: Proline-rich antimicrobial peptides (PrAMPs) internalize into susceptible bacteria using specific transporters and interfere with protein synthesis and folding. To date, mammalian PrAMPs have so far been identified only in artiodactyls. Since cetaceans are co-phyletic with artiodactyls, we mined the genome of the bottlenose dolphin Tursiops truncatus, leading to the identification of two PrAMPs, Tur1A and Tur1B. Tur1A, which is orthologous to the bovine PrAMP Bac7, is internalized into Escherichia coli, without damaging the membranes, using the inner membrane transporters SbmA and YjiL/MdM. Furthermore, like Bac7, Tur1A also inhibits bacterial protein synthesis by binding to the ribosome and blocking the transition from the initiation to the elongation phase. By contrast, Tur1B is a poor inhibitor of protein synthesis and may utilize another mechanism of action. An X-ray structure of Tur1A bound within the ribosomal exit tunnel provides a basis to develop these peptides as novel antimicrobial agents.

PubMed: 29526712
DOI: 10.1016/j.chembiol.2018.02.004

Experimental method

X-RAY DIFFRACTION (3.2 Å)