1I95

CRYSTAL STRUCTURE OF THE 30S RIBOSOMAL SUBUNIT FROM THERMUS THERMOPHILUS IN COMPLEX WITH EDEINE

Summary for 1I95

• Entry DOI: 10.2210/pdb1i95/pdb
• Related: 1FKA 1I94 1I96 1I97
• Descriptor: 16S RRNA, 30S RIBOSOMAL PROTEIN S10, 30S RIBOSOMAL PROTEIN S11, ... (25 entities in total)
• Functional Keywords: 30s ribosome, antibiotics, edeine, ribosome
• Biological source: Thermus thermophilus; More
• Total number of polymer chains: 21
• Total formula weight: 842639.23

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

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: 11296217
DOI: 10.1093/emboj/20.8.1829

Experimental method

X-RAY DIFFRACTION (4.5 Å)