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（Molecular Cell），26-38, 11 April 2008，Joerg M. Harms, Paola Fucini
Joerg M. Harms,1,2,8 Daniel N. Wilson,2,3,4,8,
Frank Schluenzen,2,5,8 Sean R. Connell,1,6 Torsten Stachelhaus,7,9 Zaneta Zaborowska,1 Christian M.T. Spahn,6 and Paola Fucini1,2,
1 Cluster of Excellence for Macromolecular Complexes, Institut für Organische Chemie und Chemische Biologie, J.W. Goethe-Universität Frankfurt am Main, Max-von-Laue-Strasse 7, D-60438 Frankfurt am Main, Germany
2 Max-Planck-Institute for Molecular Genetics, AG-Ribosomen, Ihnestrasse 73, D-14195 Berlin, Germany
3 Gene Center and Department of Chemistry and Biochemistry, University of Munich, LMU, Feodor Lynen Strasse 25, 81377 Munich, Germany
4 Munich Centre for Integrated Protein Science, University of Munich, 81377 Munich, Germany
5 Deutsches Elektronen-Synchrotron, Notkestrasse 85, D-22603 Hamburg, Germany
6 Institut für Medizinische Physik und Biophysik, Charite—Universitätsmedizin Berlin, Ziegelstrasse 5-9, 10117 Berlin, Germany
7 Department of Chemistry/Biochemistry, Philipps University of Marburg, Hans-Meerwein-Strasse, D-35032 Marburg, Germany
The thiopeptide class of antibiotics targets the GTPase-associated center (GAC) of the ribosome to inhibit translation factor function. Using X-ray crystallography, we have determined the binding sites of thiostrepton (Thio), nosiheptide (Nosi), and micrococcin (Micro), on the Deinococcus radiodurans large ribosomal subunit. The thiopeptides, by binding within a cleft located between the ribosomal protein L11 and helices 43 and 44 of the 23S rRNA, overlap with the position of domain V of EF-G, thus explaining how this class of drugs perturbs translation factor binding to the ribosome. The presence of Micro leads to additional density for the C-terminal domain (CTD) of L7, adjacent to and interacting with L11. The results suggest that L11 acts as a molecular switch to control L7 binding and plays a pivotal role in positioning one L7-CTD monomer on the G′ subdomain of EF-G to regulate EF-G turnover during protein synthesis.
