5HCQ
Crystal structure of antimicrobial peptide Oncocin d15-19 bound to the Thermus thermophilus 70S ribosome
This is a non-PDB format compatible entry.
Summary for 5HCQ
| Entry DOI | 10.2210/pdb5hcq/pdb |
| Related | 5HAU 5HCP 5HCQ 5HD1 |
| Descriptor | 23S Ribosomal RNA, 50S ribosomal protein L14, 50S ribosomal protein L15, ... (59 entities in total) |
| Functional Keywords | oncocin d15-19, antimicrobial peptide, antibiotic, 70s ribosome, inhibition of translation, peptidyl transferase inhibitors, 50s ribosomal subunit, peptide exit tunnel, ribosome-antibiotic complex, ribosome/antibiotic |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 110 |
| Total formula weight | 4465427.90 |
| Authors | Gagnon, M.G.,Roy, R.N.,Lomakin, I.B.,Florin, T.,Mankin, A.S.,Steitz, T.A. (deposition date: 2016-01-04, release date: 2016-04-06, Last modification date: 2024-03-06) |
| Primary citation | Gagnon, M.G.,Roy, R.N.,Lomakin, I.B.,Florin, T.,Mankin, A.S.,Steitz, T.A. Structures of proline-rich peptides bound to the ribosome reveal a common mechanism of protein synthesis inhibition. Nucleic Acids Res., 44:2439-2450, 2016 Cited by PubMed Abstract: With bacterial resistance becoming a serious threat to global public health, antimicrobial peptides (AMPs) have become a promising area of focus in antibiotic research. AMPs are derived from a diverse range of species, from prokaryotes to humans, with a mechanism of action that often involves disruption of the bacterial cell membrane. Proline-rich antimicrobial peptides (PrAMPs) are instead actively transported inside the bacterial cell where they bind and inactivate specific targets. Recently, it was reported that some PrAMPs, such as Bac71 -35, oncocins and apidaecins, bind and inactivate the bacterial ribosome. Here we report the crystal structures of Bac71 -35, Pyrrhocoricin, Metalnikowin and two oncocin derivatives, bound to the Thermus thermophilus 70S ribosome. Each of the PrAMPs blocks the peptide exit tunnel of the ribosome by simultaneously occupying three well characterized antibiotic-binding sites and interferes with the initiation step of translation, thereby revealing a common mechanism of action used by these PrAMPs to inactivate protein synthesis. Our study expands the repertoire of PrAMPs and provides a framework for designing new-generation therapeutics. PubMed: 26809677DOI: 10.1093/nar/gkw018 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.801 Å) |
Structure validation
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