Wolf Prize Laureate in Chemistry 2006/7
Affiliation at the time of the award:
Weizmann Institute of Science, Israel
“for ingenious structural discoveries of the ribosomal machinery of peptide-bond formation and the light-driven primary processes in photosynthesis”.
The work of both scientists has led to a unified picture of basic biological machinery. Ada Yonath was the first to determine against all odds the structure of the ribosome, which is the large protein-synthesis machinery of living cells. George Feher pioneered the structure/function relations of the simplest reaction centre in photosynthesis, revealing the basic principles of light energy conversion in biology.
The ribosome is the universal mega-Dalton highly complex riboprotein assembly that translates the genetic code into proteins. The recent emergence of ribosome structures in the crystallographic community is mainly due to Ada Yonath, who uniquely and single-handedly pioneered ribosomal crystallography over more than two decades ago, when others could not even conceive its possibility. By pushing crystallography to its limits, she demonstrated the feasibility of ribosomal crystallography, thus inspiring prominent groups to repeat her experiments. Throughout, she has been the leading force in all stages of structure determination and has introduced fundamental methodological innovations that have greatly impacted the entire field of structural biology.
Yonath´s achievements in protein crystallography were based on the introduction of state-of-the-art ultra-cold bio-crystallography, an innovative method for minimizing the extreme sensitivity of the ribosomal crystal to irradiation. Yonath’s strength, persistence, skills and daring in approaching problems considered insurmountable at the time, let her to explore new experimental and conceptual approaches, later adopted by the scientific community at large.
Ada Yonath was the first to discover the unified ribosomal mechanism leading to the production of proteins. However, Ada Yonath´s recent endeavour also comprises applied aspects, as it sheds light on targeting antibiotics toward a ribosome complex. She is the first and only person to determine, in an incredibly short time, the structures of over a dozen different complexes of antibiotics, reveal the ribosome-antibiotics binding sites on the molecular level and provide insight into antibiotics selectivity.
Her work paves the way to deal with the crucial issue of drug activity and resistance mechanisms, thus touching on a central problem in medicine.