A newly-discovered arsenic-containing compound produced by a soil bacterium shows promise as a broad-spectrum antibiotic. In a paper published in the Nature journal Communications Biology, an international team of researchers demonstrated that arsinothricin (AST) is effective against many types of gram-negative and gram-positive bacteria. The effort was led by Barry Rosen of the Florida International University College of Medicine and Masafumi Yoshinaga of the National Agriculture and Food Research Organization (NARO) in Japan. Banumathi Sankaran, a research scientist in the Berkeley Center for Structural Biology (BSCB) at the Advanced Light Source (ALS), was an author on the paper.
The Helical Carotenoid Protein 2 (HCP2) protein is an ancestor of proteins that are known to protect against damage caused by excess light exposure. Researchers in the laboratory of Cheryl Kerfeld, guest faculty in the Environmental Genomics & Systems Biology (EGSB) Division, are the first to structurally and biophysically analyze a protein from the HCP family. This HCP protein family was discovered recently by Kerfeld and the members of her lab, who are based in EGSB and at Michigan State University (MSU). To solve the molecular structure of HCP2, X-ray diffraction was measured at beam line 5.0.2 in the Berkeley Center for Structural Biology of the Advanced Light Source (ALS). The structure was refined using Phenix, a software suite for automated determination of molecular structures developed under the direction of Paul Adams, Molecular Biophysics and Integrated Bioimaging Division Director. Read more in the MSU-DOE Plant Research Laboratory news story.
Mutations in the proteins that regulate cellular processes such as growth, division, and death are often linked to cancer and other diseases. The proper function of one of these proteins, SHP2, depends on maintaining equilibrium in a structural tug-of-war between an open (active) and a closed (inactive) arrangement. A team of researchers from Brandeis University performed X-ray crystallography at Advanced Light Source (ALS) Beamlines 8.2.1 and 8.2.2—part of the Berkeley Center for Structural Biology—to elucidate the structures of healthy and mutated forms of SHP2 and the dynamic interchange between their open and closed conformations, as well as how SHP2 interacts with certain cancer drugs.
Read more in this ALS Science Highlight.
A team led by Mary Estes of the Baylor College of Medicine used rotavirus as a model to study some of the proteins involved in making the cytoplasmic compartments in which many DNA and RNA virus pathogens replicate. Banumathi Sankaran, a research scientist in the Berkeley Center for Structural Biology (BSCB) at the Advanced Light Source, collected the X-ray data at the BCSB Beamline 5.0.1 that were used to solve the three-dimensional structures of nonstructural protein NSP2. Understanding the functions of proteins that make these compartments could offer an avenue for disrupting virus production. The team published their findings in Proceedings of the National Academy of Sciences.
Bioscientists at the Advanced Light Source (ALS) at Berkeley Lab lent their expertise to a project led by scientists at the University of Washington to design proteins in the lab that zip together like DNA. The technique could enable the design of protein nanomachines to help diagnose and treat disease, allow for more precise engineering of cells, and perform a variety of other tasks.