3BBU
The Hsp15 protein fitted into the low resolution Cryo-EM map of the 50S.nc-tRNA.Hsp15 complex
Summary for 3BBU
| Entry DOI | 10.2210/pdb3bbu/pdb |
| Related | 1DM9 3BBV 3BBX |
| EMDB information | 1455 |
| Descriptor | Heat Shock Protein 15 (1 entity in total) |
| Functional Keywords | alpha-l rna binding, heat shock, rescue stalled ribosome, ribosome |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 11901.72 |
| Authors | Jiang, L.,Abrahams, J.P. (deposition date: 2007-11-11, release date: 2008-10-21, Last modification date: 2024-02-21) |
| Primary citation | Jiang, L.,Schaffitzel, C.,Bingel-Erlenmeyer, R.,Ban, N.,Korber, P.,Koning, R.I.,de Geus, D.C.,Plaisier, J.R.,Abrahams, J.P. Recycling of Aborted Ribosomal 50S Subunit-Nascent Chain-tRNA Complexes by the Heat Shock Protein Hsp15. J.Mol.Biol., 386:1357-1367, 2009 Cited by PubMed Abstract: When heat shock prematurely dissociates a translating bacterial ribosome, its 50S subunit is prevented from reinitiating protein synthesis by tRNA covalently linked to the unfinished protein chain that remains threaded through the exit tunnel. Hsp15, a highly upregulated bacterial heat shock protein, reactivates such dead-end complexes. Here, we show with cryo-electron microscopy reconstructions and functional assays that Hsp15 translocates the tRNA moiety from the A site to the P site of stalled 50S subunits. By stabilizing the tRNA in the P site, Hsp15 indirectly frees up the A site, allowing a release factor to land there and cleave off the tRNA. Such a release factor must be stop codon independent, suggesting a possible role for a poorly characterized class of putative release factors that are upregulated by cellular stress, lack a codon recognition domain and are conserved in eukaryotes. PubMed: 19013177DOI: 10.1016/j.jmb.2008.10.079 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (10 Å) |
Structure validation
Download full validation report
