8R8M
70S Escherichia coli ribosome with Paenilamicin B2 bound with hybrid A/P- and hybrid P/E-tRNA.
This is a non-PDB format compatible entry.
Summary for 8R8M
Entry DOI | 10.2210/pdb8r8m/pdb |
Related | 8R6C 9FBV |
EMDB information | 19004 |
Related PRD ID | PRD_002555 |
Descriptor | Large ribosomal subunit protein bL33, Large ribosomal subunit protein uL6, Large ribosomal subunit protein bL9, ... (60 entities in total) |
Functional Keywords | ribosome, 70s, paenilamicin, antibiotic |
Biological source | Escherichia coli BW25113 More |
Total number of polymer chains | 56 |
Total formula weight | 2201656.74 |
Authors | |
Primary citation | Koller, T.O.,Berger, M.J.,Morici, M.,Paternoga, H.,Bulatov, T.,Di Stasi, A.,Dang, T.,Mainz, A.,Raulf, K.,Crowe-McAuliffe, C.,Scocchi, M.,Mardirossian, M.,Beckert, B.,Vazquez-Laslop, N.,Mankin, A.,Sussmuth, R.D.,Wilson, D.N. Paenilamicins from the honey bee pathogen Paenibacillus larvae are context-specific translocation inhibitors of protein synthesis. Biorxiv, 2024 Cited by PubMed Abstract: The paenilamicins are a group of hybrid non-ribosomal peptide-polyketide compounds produced by the honey bee pathogen that display activity against Gram-positive pathogens, such as . While paenilamicins have been shown to inhibit protein synthesis, their mechanism of action has remained unclear. Here, we have determined structures of the paenilamicin PamB2 stalled ribosomes, revealing a unique binding site on the small 30S subunit located between the A- and P-site tRNAs. In addition to providing a precise description of interactions of PamB2 with the ribosome, the structures also rationalize the resistance mechanisms utilized by . We could further demonstrate that PamB2 interferes with the translocation of mRNA and tRNAs through the ribosome during translation elongation, and that this inhibitory activity is influenced by the presence of modifications at position 37 of the A-site tRNA. Collectively, our study defines the paenilamicins as a new class of context-specific translocation inhibitors. PubMed: 38826346DOI: 10.1101/2024.05.21.595107 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.4 Å) |
Structure validation
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