A team led by Eva Nogales, senior faculty scientist in the Molecular Biophysics and Integrated Bioimaging (MBIB) Division, has produced the first detailed 3D structure of human SAGA, a 20-piece molecular machine that’s crucial to life. The structure, reported in Nature Structural & Molecular Biology, revealed some unexpected differences between the human and yeast versions of SAGA and could guide the development of drugs to treat diseases that arise when this complex malfunctions.
Nogales Appointed to Royal Academy of Spain
Eva Nogales, a senior faculty scientist in the Molecular Biophysics and Integrated Bioimaging (MBIB) Division, was appointed as a foreign member attached to the Natural Sciences Section of the Royal Academy of Exact, Physical, and Natural Sciences of Spain. The Royal Academy, founded in 1847, is tasked with promoting study and research in the mathematical, physical, chemical, geological, and biological sciences, as well as disseminating the knowledge gained thereby. It is made up of a maximum of 72 permanent members, 144 corresponding members, and supernumerary members and foreign members. Nogales, who is also a Howard Hughes Medical Institute (HHMI) investigator and professor at UC Berkeley, obtained her bachelor’s degree in physics from the Universidad Autonoma de Madrid in Spain. Her research specialty involves using electron microscopy (EM) and image analysis, as well as biochemical and biophysical assays to gain mechanistic insights into crucial molecular processes in the life of eukaryotic cells.
BCSB Determines Interactions of Potential Inhibitor with SARS-CoV-2 Protease
Researchers from the Baylor College of Medicine employed previously constructed DNA-encoded chemistry technology (DEC-tec) libraries to identify several candidate molecules that could inhibit the action of Mpro, the main protease of SARS-CoV-2. In a recent study, the researchers described CDD-1713, a new inhibitor to the enzyme Mpro that is involved in propagating the virus. The X-ray crystallographic data, which was collected by Banumathi Sankaran in the Molecular Biophysics and Integrated Bioimaging Division, allowed the researchers to determine that CDD-1713 inhibits the activity of Mpro by binding in the active site of this enzyme.
A New Way to Make Chemicals Not Found in Nature
Synthetic biologists have successfully engineered microbes to make chemicals cheaply and more sustainably. However, researchers have been limited by the fact that microbes can only make molecules using chemical reactions seen in nature.
A collaboration between scientists at Berkeley Lab and UC Berkeley has engineered the microbe E. coli to produce a molecule that, until now, could only be synthesized in a laboratory.
New Technique Gets the Drop On Enzyme Reactions
As part of an international collaboration, researchers at Lawrence Berkeley National Laboratory (Berkeley Lab), the Diamond Light Source synchrotron facility, and Oxford and Bristol Universities in England have developed a novel sample delivery system that expands the limited toolkit for performing dynamic structural biology studies of enzyme catalysis, which have so far mostly been limited to a small number of light-driven enzymes.
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