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TitleCryo-EM structures of a bathy phytochrome histidine kinase reveal a unique light-dependent activation mechanism.
Journal, issue, pagesStructure, Year 2024
Publish dateAug 23, 2024
AuthorsSzabolcs Bódizs / Petra Mészáros / Lukas Grunewald / Heikki Takala / Sebastian Westenhoff /
PubMed AbstractPhytochromes are photoreceptor proteins in plants, fungi, and bacteria. They can adopt two photochromic states with differential biochemical responses. The structural changes transducing the signal ...Phytochromes are photoreceptor proteins in plants, fungi, and bacteria. They can adopt two photochromic states with differential biochemical responses. The structural changes transducing the signal from the chromophore to the biochemical output modules are poorly understood due to challenges in capturing structures of the dynamic, full-length protein. Here, we present cryoelectron microscopy (cryo-EM) structures of the phytochrome from Pseudomonas aeruginosa (PaBphP) in its resting (Pfr) and photoactivated (Pr) state. The kinase-active Pr state has an asymmetric, dimeric structure, whereas the kinase-inactive Pfr state opens up. This behavior is different from other known phytochromes and we explain it with the unusually short connection between the photosensory and output modules. Multiple sequence alignment of this region suggests evolutionary optimization for different modes of signal transduction in sensor proteins. The results establish a new mechanism for light-sensing by phytochrome histidine kinases and provide input for the design of optogenetic phytochrome variants.
External linksStructure / PubMed:39216473
MethodsEM (single particle)
Resolution2.95 - 4.3 Å
Structure data

EMDB-19981, PDB-9eut:
Cryo-EM structure of the full-length Pseudomonas aeruginosa bacteriophytochrome in its Pr state
Method: EM (single particle) / Resolution: 2.95 Å

EMDB-19989, PDB-9euy:
Cryo-EM structure of the full-length Pseudomonas aeruginosa bacteriophytochrome in its Pfr state
Method: EM (single particle) / Resolution: 2.95 Å

EMDB-50007: Consensus refinement of the full-length Pseudomonas aeruginosa bacteriophytochrome in its Pr state
Method: EM (single particle) / Resolution: 3.8 Å

EMDB-50008: Local refinement of the full-length Pseudomonas aeruginosa bacteriophytochrome in its Pr state
Method: EM (single particle) / Resolution: 2.95 Å

EMDB-50009: Local refinement of the full-length Pseudomonas aeruginosa bacteriophytochrome in its Pr state
Method: EM (single particle) / Resolution: 4.3 Å

Chemicals

ChemComp-LBV:
3-[2-[(Z)-[3-(2-carboxyethyl)-5-[(Z)-(4-ethenyl-3-methyl-5-oxidanylidene-pyrrol-2-ylidene)methyl]-4-methyl-pyrrol-1-ium

Source
  • pseudomonas aeruginosa (bacteria)
KeywordsCYTOSOLIC PROTEIN / Photosensor / Photoreceptor / Phytochrome / Bacterial protein

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