5UQ7
70S ribosome complex with dnaX mRNA stemloop and E-site tRNA ("in" conformation)
This is a non-PDB format compatible entry.
Summary for 5UQ7
Entry DOI | 10.2210/pdb5uq7/pdb |
Related | 5UQ8 |
EMDB information | 8596 8597 |
Descriptor | 23S rRNA, 50S ribosomal protein L14, 50S ribosomal protein L15, ... (58 entities in total) |
Functional Keywords | 70s ribosome, dnax, stem-loop, structured mrna, -1 programmed frameshifting, e site, ribosome |
Biological source | Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) More |
Total number of polymer chains | 56 |
Total formula weight | 2231460.70 |
Authors | Zhang, Y.,Hong, S.,Skiniotis, G.,Dunham, C.M. (deposition date: 2017-02-07, release date: 2018-03-07, Last modification date: 2025-03-19) |
Primary citation | Zhang, Y.,Hong, S.,Ruangprasert, A.,Skiniotis, G.,Dunham, C.M. Alternative Mode of E-Site tRNA Binding in the Presence of a Downstream mRNA Stem Loop at the Entrance Channel. Structure, 26:437-445.e3, 2018 Cited by PubMed Abstract: Structured mRNAs positioned downstream of the ribosomal decoding center alter gene expression by slowing protein synthesis. Here, we solved the cryo-EM structure of the bacterial ribosome bound to an mRNA containing a 3' stem loop that regulates translation. Unexpectedly, the E-site tRNA adopts two distinct orientations. In the first structure, normal interactions with the 50S and 30S E site are observed. However, in the second structure, although the E-site tRNA makes normal interactions with the 50S E site, its anticodon stem loop moves ∼54 Å away from the 30S E site to interact with the 30S head domain and 50S uL5. This position of the E-site tRNA causes the uL1 stalk to adopt a more open conformation that likely represents an intermediate state during E-site tRNA dissociation. These results suggest that structured mRNAs at the entrance channel restrict 30S subunit movement required during translation to slow E-site tRNA dissociation. PubMed: 29456023DOI: 10.1016/j.str.2018.01.013 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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