Activation Of Signaling Protein Is Visualized

Abstract

Researchers have devised a way to watch a light-induced signaling protein as it functions, revealing new details about the way it is activated to do its job. The technique could make it possible to better understand step-by-step mechanisms of other signaling proteins, which control processes such as the movement of leaves toward light and vision in higher animals, and possibly the mechanisms of enzymes as well. In the study, the researchers used time-resolved Laue crystallography to take structural snapshots of bacterial photoactive yellow protein (PYP) in action. When PYP is activated by potentially harmful light frequencies, it provides signals that induce the bacteria to swim away. Using the Laue method, which harnesses polychromatic X-ray pulses to rapidly obtain structural information from protein crystals, the researchers captured PYP’s activation with near-atomic spatial resolution and 150-picosecond time resolution. Ultrafast biophysical chemistry specialist Philip A. Anfinrud of the National Inst...