8AP4
Structure of Escherischia coli heat shock protein Hsp15 in complex with ribosomal 50S subunits bearing peptidyl-tRNA
Summary for 8AP4
| Entry DOI | 10.2210/pdb8ap4/pdb |
| EMDB information | 15558 |
| Descriptor | 50S ribosomal protein L33, 50S ribosomal protein L2, 50S ribosomal protein L3, ... (33 entities in total) |
| Functional Keywords | s4 domain, heat shock, stress response, ribosome quality control, translation |
| Biological source | Escherichia coli K-12 More |
| Total number of polymer chains | 33 |
| Total formula weight | 1390649.36 |
| Authors | Safdari, H.A.,Wilson, D.N. (deposition date: 2022-08-09, release date: 2022-11-16, Last modification date: 2022-12-28) |
| Primary citation | Safdari, H.A.,Kasvandik, S.,Polte, C.,Ignatova, Z.,Tenson, T.,Wilson, D.N. Structure of Escherichia coli heat shock protein Hsp15 in complex with the ribosomal 50S subunit bearing peptidyl-tRNA. Nucleic Acids Res., 50:12515-12526, 2022 Cited by PubMed Abstract: In Escherichia coli, the heat shock protein 15 (Hsp15) is part of the cellular response to elevated temperature. Hsp15 interacts with peptidyl-tRNA-50S complexes that arise upon dissociation of translating 70S ribosomes, and is proposed to facilitate their rescue and recycling. A previous structure of E. coli Hsp15 in complex with peptidyl-tRNA-50S complex reported a binding site located at the central protuberance of the 50S subunit. By contrast, recent structures of RqcP, the Hsp15 homolog in Bacillus subtilis, in complex with peptidyl-tRNA-50S complexes have revealed a distinct site positioned between the anticodon-stem-loop (ASL) of the P-site tRNA and H69 of the 23S rRNA. Here we demonstrate that exposure of E. coli cells to heat shock leads to a decrease in 70S ribosomes and accumulation of 50S subunits, thus identifying a natural substrate for Hsp15 binding. Additionally, we have determined a cryo-EM reconstruction of the Hsp15-50S-peptidyl-tRNA complex isolated from heat shocked E. coli cells, revealing that Hsp15 binds to the 50S-peptidyl-tRNA complex analogously to its B. subtilis homolog RqcP. Collectively, our findings support a model where Hsp15 stabilizes the peptidyl-tRNA in the P-site and thereby promotes access to the A-site for putative rescue factors to release the aberrant nascent polypeptide chain. PubMed: 36370110DOI: 10.1093/nar/gkac1035 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3 Å) |
Structure validation
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