Ada Yonath

Weizmann Institute of Science

Primary Section: 29, Biophysics and Computational Biology
Secondary Section: 21, Biochemistry
Membership Type:
International Member (elected 2003)


Ada Yonath is focusing on protein biosynthesis, on antibiotics hampering it, on human diseases associated with ribosomal mutations and on the origin of life. She is the Director of Kimmelman Center for Biomolecular-Structures at the Weizmann Institute (WIS), where she got her PhD and currently is a faculty member. She was a post-doc in Carnegie Mellon, MIT and U. Chicago. In the seventies she established at WIS the first structural-biology laboratory in Israel, which was the only one in the country for almost a decade. During 1986-2004 she headed Max-Planck-Research-Unit for Ribosome Structure in Hamburg in parallel to her WIS activities.   Among others, she is a member of US-National Academy; the British Royal Society; the Israel Academy; the  German Leopoldina; the Pontificia Accademia-delle-Scienze (Vatican); the Korean Science Academy; the European Academy; the European Molecular Biology Organization; and holds honorary doctorates from over 45 Universities worldwide, and almost all in Israel. Her awards include Louisa-Gross-Horwitz Prize, Wolf Prize; Harvey Prize; Israel Prizes; Linus-Pauling Gold Medal; UNESCO/L’Oreal Award; Albert-Einstein Award for Excellence; and the 2009 Nobel Prize for Chemistry. 

Research Interests

As a structural biologist, I have been focusing on protein biosynthesis mechanisms, using ribosomal crystallography, a research line pioneered by my research team in the beginning of the eighties. We identified eubacterial ribosomes crystallizable under conditions allowing optimal functional activity, which yielded complete high-resolution structures of functionally relevant conformations of both ribosomal subunits. Consequently we discovered a sizable symmetry related region within the otherwise asymmetric ribosome, and revealed the parameters crucial for precise substrates placement. A thorough analysis confirmed that the ribosome contributes positional catalysis to its dual tasks: peptide bond formation and aminoacid polymerization. We discovered the unified ribosomal machinery for peptide-bond formation, translocation and nascent protein progression into their exit tunnel. This tunnel, visualized by us in the mid-eighties, is one of the main targets for antibiotics. As we are focusing on species proved to be suitable pathogen models, we elucidated modes of action of over twenty different antibiotics, belonging to a dozen different antibiotic-families, all complexed with ribosomes at clinically relevant concentrations. Further analysis provided the structural bases for antibiotics synergism, clarified antibiotics selectivity and illuminated resistance mechanisms, thus paving the way for structural based drug design. We also identified structural elements allowing the tunnel's dynamic, thus enabling ribosomal involvement in discrimination and intra-cellular regulation.

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