1I96
CRYSTAL STRUCTURE OF THE 30S RIBOSOMAL SUBUNIT FROM THERMUS THERMOPHILUS IN COMPLEX WITH THE TRANSLATION INITIATION FACTOR IF3 (C-TERMINAL DOMAIN)
Summary for 1I96
| Entry DOI | 10.2210/pdb1i96/pdb |
| Related | 1FKA 1I94 1I95 1I97 1TIG |
| Descriptor | 16S RRNA, 30S RIBOSOMAL PROTEIN S10, 30S RIBOSOMAL PROTEIN S11, ... (25 entities in total) |
| Functional Keywords | 30s ribosome, translation initiation factor, if3, ribosome |
| Biological source | Thermus thermophilus More |
| Total number of polymer chains | 22 |
| Total formula weight | 843490.52 |
| Authors | Pioletti, M.,Schluenzen, F.,Harms, J.,Zarivach, R.,Gluehmann, M.,Avila, H.,Bartels, H.,Jacobi, C.,Hartsch, T.,Yonath, A.,Franceschi, F. (deposition date: 2001-03-18, release date: 2001-04-12, Last modification date: 2024-02-07) |
| Primary citation | Pioletti, M.,Schlunzen, F.,Harms, J.,Zarivach, R.,Gluhmann, M.,Avila, H.,Bashan, A.,Bartels, H.,Auerbach, T.,Jacobi, C.,Hartsch, T.,Yonath, A.,Franceschi, F. Crystal structures of complexes of the small ribosomal subunit with tetracycline, edeine and IF3. EMBO J., 20:1829-1839, 2001 Cited by PubMed Abstract: The small ribosomal subunit is responsible for the decoding of genetic information and plays a key role in the initiation of protein synthesis. We analyzed by X-ray crystallography the structures of three different complexes of the small ribosomal subunit of Thermus thermophilus with the A-site inhibitor tetracycline, the universal initiation inhibitor edeine and the C-terminal domain of the translation initiation factor IF3. The crystal structure analysis of the complex with tetracycline revealed the functionally important site responsible for the blockage of the A-site. Five additional tetracycline sites resolve most of the controversial biochemical data on the location of tetracycline. The interaction of edeine with the small subunit indicates its role in inhibiting initiation and shows its involvement with P-site tRNA. The location of the C-terminal domain of IF3, at the solvent side of the platform, sheds light on the formation of the initiation complex, and implies that the anti-association activity of IF3 is due to its influence on the conformational dynamics of the small ribosomal subunit. PubMed: 11296217DOI: 10.1093/emboj/20.8.1829 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (4.2 Å) |
Structure validation
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