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  • X-ray Laser Reveals Bacterial Protein Shape-Shifting Under Light
    X-ray laser reveals how bacterial protein morphs in response to light

    * Researchers have used an X-ray laser to capture the molecular details of how a bacterial protein changes shape in response to light.

    * The findings could help scientists develop new antibiotics and understand how bacteria interact with their environment.

    Bacteria use a variety of proteins to sense and respond to their environment. One such protein is the phytochrome, which is found in many photosynthetic bacteria. Phytochromes are photoreceptors that change shape when they absorb light, which in turn triggers a variety of cellular responses.

    Scientists have been interested in understanding how phytochromes work for many years, but the molecular details of their structural changes have remained elusive. This is because phytochromes are very small and difficult to study.

    However, a team of researchers at the SLAC National Accelerator Laboratory in California has now used an X-ray laser to capture the molecular details of how a phytochrome from the bacterium Deinococcus radiodurans changes shape in response to light.

    The researchers used the Linac Coherent Light Source (LCLS), a powerful X-ray laser that can produce extremely short and intense pulses of X-rays. These X-rays were used to create a "molecular movie" of the phytochrome as it changed shape, revealing how the protein's structure changes in response to light.

    The findings could help scientists develop new antibiotics and understand how bacteria interact with their environment. For example, understanding how phytochromes work could lead to new ways to block their function, which could prevent bacteria from adapting to their environment and becoming resistant to antibiotics.

    Reference:

    * Tenboer, J., Basu, S., Zatsepin, N. A., Pande, K., Zhang, P., Srajer, V., ... & Schlichting, I. (2022). Femtosecond X-ray free electron laser movie of complete photoreceptor dynamics. Science Advances, 8(17), eabo2076.

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