4V4P
Crystal structure of 70S ribosome with thrS operator and tRNAs.
This is a non-PDB format compatible entry.
Summary for 4V4P
| Entry DOI | 10.2210/pdb4v4p/pdb |
| Related | 1YL4 1giy 1nkw |
| Descriptor | 5S ribosomal RNA, 50S ribosomal protein L9, 50S ribosomal protein L11, ... (56 entities in total) |
| Functional Keywords | ribosome, mrna, translational operator |
| Biological source | Thermus thermophilus More |
| Total number of polymer chains | 58 |
| Total formula weight | 2308735.78 |
| Authors | Jenner, L.,Romby, P.,Rees, B.,Schulze-Briese, C.,Springer, M.,Ehresmann, C.,Ehresmann, B.,Moras, D.,Yusupova, G.,Yusupov, M. (deposition date: 2005-01-19, release date: 2014-07-09, Last modification date: 2024-10-30) |
| Primary citation | Jenner, L.,Romby, P.,Rees, B.,Schulze-Briese, C.,Springer, M.,Ehresmann, C.,Ehresmann, B.,Moras, D.,Yusupova, G.,Yusupov, M. Translational operator of mRNA on the ribosome: how repressor proteins exclude ribosome binding. Science, 308:120-123, 2005 Cited by PubMed Abstract: The ribosome of Thermus thermophilus was cocrystallized with initiator transfer RNA (tRNA) and a structured messenger RNA (mRNA) carrying a translational operator. The path of the mRNA was defined at 5.5 angstroms resolution by comparing it with either the crystal structure of the same ribosomal complex lacking mRNA or with an unstructured mRNA. A precise ribosomal environment positions the operator stem-loop structure perpendicular to the surface of the ribosome on the platform of the 30S subunit. The binding of the operator and of the initiator tRNA occurs on the ribosome with an unoccupied tRNA exit site, which is expected for an initiation complex. The positioning of the regulatory domain of the operator relative to the ribosome elucidates the molecular mechanism by which the bound repressor switches off translation. Our data suggest a general way in which mRNA control elements must be placed on the ribosome to perform their regulatory task. PubMed: 15802605DOI: 10.1126/science.1105639 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (5.5 Å) |
Structure validation
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