西亚试剂：Translational Regulation via L11: Molecular Switches on the

发布时间：2026-02-21

（Molecular Cell），26-38, 11 April 2008，Joerg M. Harms, Paola Fucini

Translational Regulation via L11: Molecular Switches on the Ribosome Turned On and Off by Thiostrepton and Micrococcin

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,

¹Cluster 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
²Max-Planck-Institute for Molecular Genetics, AG-Ribosomen, Ihnestrasse 73, D-14195 Berlin, Germany
³Gene Center and Department of Chemistry and Biochemistry, University of Munich, LMU, Feodor Lynen Strasse 25, 81377 Munich, Germany
⁴Munich Centre for Integrated Protein Science, University of Munich, 81377 Munich, Germany
⁵Deutsches Elektronen-Synchrotron, Notkestrasse 85, D-22603 Hamburg, Germany
⁶Institut für Medizinische Physik und Biophysik, Charite—Universitätsmedizin Berlin, Ziegelstrasse 5-9, 10117 Berlin, Germany
⁷Department of Chemistry/Biochemistry, Philipps University of Marburg, Hans-Meerwein-Strasse, D-35032 Marburg, Germany

Summary

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.

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