Crystal structures of complexes of the small ribosomal subunit with tetracycline, edeine and IF3

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 inhi...

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Bibliographic Details
Published in:The EMBO journal 2001-04, Vol.20 (8), p.1829-1839
Main Authors: Pioletti, Marta, Schlünzen, Frank, Harms, Jörg, Zarivach, Raz, Glühmann, Marco, Avila, Horacio, Bashan, Anat, Bartels, Heike, Auerbach, Tamar, Jacobi, Carsten, Hartsch, Thomas, Yonath, Ada, Franceschi, François
Format: Article
Language:English
Subjects:
antibiotics
Binding Sites
Crystallography, X-Ray
edeine
Edeine - chemistry
Eukaryotic Initiation Factor-3
IF3
initiation factor IF-3
Models, Molecular
Peptide Chain Initiation, Translational
Peptide Initiation Factors - chemistry
Protein Synthesis Inhibitors - chemistry
ribosomes
Ribosomes - chemistry
tetracycline
Tetracycline - chemistry
Thermus thermophilus
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Summary: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.
ISSN:0261-4189
1460-2075
1460-2075
DOI:10.1093/emboj/20.8.1829