Dr. Thomas A. Steitz, 2009 Nobel Laureate in Chemistry, Sterling Professor of Molecular Biophysics and Biochemistry, Howard Hughes Medical Institute Investigator, Yale University, is the recipient of Shideman-Sterling lectureship for 2011. He will be on campus on October 10, 2011 to present his work on ribosome structure.

Dr. Steitz and colleagues have been pursuing high-resolution structural studies of the ribosome, the machine that synthesizes proteins and have determined the atomic structure of the 1.6-mDa ribosomal subunit that catalyzes the formation of the peptide bond.
The structures of the large subunit with either substrate or product analogs bound to the active site of peptide synthesis provide insights into the molecular mechanisms of protein synthesis and show that the peptidyltransferase center is made entirely of RNA.
They have also established the structures of nearly two dozen different antibiotics that target the large ribosomal subunit in complex with the large subunit as well as complexes with a T. thermophilus 70S ribosome, including two members of the tuberactinomycin family of antibiotics that are used to treat tuberculosis. These structures not only establish how these antibiotics stop peptide synthesis but also are providing the basis for structure-based design of new antibiotics that are effective against ribosomes containing antibiotic-resistance mutations.
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