Researchers have discovered the structure of a well-established target for antibiotic development, an enzyme called MraY, as it is bound to the natural antibacterial muraymycin. The enzyme dramatically changes its shape to reveal a hidden binding pocket, which muraymycin connects to like a two-pronged plug inserting into a socket. “Nature has evolved a number of ways to inhibit this enzyme, but researchers haven’t been able to mimic their properties in the laboratory,” said senior study author Seok-Yong Lee, PhD, assistant professor of biochemistry at Duke University School of Medicine. “Here, we provide a platform for understanding how these natural inhibitors work, with the degree of molecular detail necessary to accelerate drug development.” Read more