Ubiquitous Structural Signaling in Bacterial Phytochromes

• The phytochrome family of light-switchable proteins has long been studied by biochemical, spectroscopic and crystallographic means, while a direct probe for global conformational signal propagation has been lacking. Using solution X-ray scattering, we find that the photosensory cores of several bacterial phytochromes undergo similar large-scale structural changes upon red-light excitation. The data establish that phytochromes with ordinary and inverted photocycles share a structural signaling mechanism and that a particular conserved histidine, previously proposed to be involved in signal propagation, in fact tunes photoresponse.

Subject headings

NATURVETENSKAP  -- Kemi (hsv//swe)

NATURAL SCIENCES  -- Chemical Sciences (hsv//eng)

NATURVETENSKAP  -- Fysik (hsv//swe)

NATURAL SCIENCES  -- Physical Sciences (hsv//eng)

NATURVETENSKAP  -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)

NATURAL SCIENCES  -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)

Keyword

AGROBACTERIUM-TUMEFACIENS C58

CHROMOPHORE-BINDING DOMAIN

HISTIDINE

KINASES

CRYSTAL-STRUCTURE

SCATTERING DATA

BACTERIOPHYTOCHROME

LIGHT

DYNAMICS

REVEALS

SWITCH

Chemistry

Physical

Nanoscience & Nanotechnology

Materials Science

Multidisciplinary

Physics

Atomic

Molecular & Chemical

Publication and Content Type

ref (subject category)

art (subject category)