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Just out: A bacteriophytochrome Pr/Pfr heterodimer studied through single-particle time-resolved cryo-electron microscopy
Communications Chemistry, Published online: 08 June 2026; doi:10.1038/s42004-026-02084-6The transition of bacterial phytochromes from the red-absorbing Pr state to the far-red-absorbing Pfr state may proceed through the formation of a Pr/Pfr heterodimer, as revealed by a recent single-particle cryo-EM study of a phytochrome from the myxobacterium Stigmatella aurantiaca. By illuminating this protein immediately before vitrification, the authors captured the Pr/Pfr heterodimer intermediate on a millisecond timescale and observed a large rotation of the C-terminal histidine kinase domain, a conformational change that is likely to regulate light-induced signal transduction.dlvr.it
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A bacteriophytochrome Pr/Pfr heterodimer studied through single-particle time-resolved cryo-electron microscopy
Communications Chemistry