Structural basis for light control of cell development revealed by crystal structures of a myxobacterial phytochrome
Woitowich, N. C., Halavaty, A. S., Waltz, P., Kupitz, C., Valera, J., Tracy, G., Gallagher, K. D., Claesson, E., Nakane, T., Pandey, S., Nelson, G., Tanaka, R., Nango, E., Mizohata, E., Owada, S., Tono, K., Joti, Y., Nugent, A. C., Patel, H., . . . Stojković, E. A. (2018). Structural basis for light control of cell development revealed by crystal structures of a myxobacterial phytochrome. IUCrJ, 5(5), 619-634. https://doi.org/10.1107/S2052252518010631
© 2018 the Authors
Phytochromes are red-light photoreceptors that were first characterized in plants, with homologs in photosynthetic and non-photosynthetic bacteria known as bacteriophytochromes (BphPs). Upon absorption of light, BphPs interconvert between two states denoted Pr and Pfr with distinct absorption spectra in the red and far-red. They have recently been engineered as enzymatic photoswitches for fluorescent-marker applications in non-invasive tissue imaging of mammals. This article presents cryo- and room-temperature crystal structures of the unusual phytochrome from the non-photosynthetic myxobacterium Stigmatella aurantiaca (SaBphP1) and reveals its role in the fruiting-body formation of this photomorphogenic bacterium. SaBphP1 lacks a conserved histidine (His) in the chromophore-binding domain that stabilizes the Pr state in the classical BphPs. Instead it contains a threonine (Thr), a feature that is restricted to several myxobacterial phytochromes and is not evolutionarily understood. SaBphP1 structures of the chromophore binding domain (CBD) and the complete photosensory core module (PCM) in wild-type and Thr-to-His mutant forms reveal details of the molecular mechanism of the Pr/Pfr transition associated with the physiological response of this myxobacterium to red light. Specifically, key structural differences in the CBD and PCM between the wild-type and the Thr-to-His mutant involve essential chromophore contacts with proximal amino acids, and point to how the photosignal is transduced through the rest of the protein, impacting the essential enzymatic activity in the photomorphogenic response of this myxobacterium. ...
PublisherInternational Union of Crystallography
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Related funder(s)Academy of Finland
Funding program(s)Academy Project, AoF
Additional information about fundingThis work was supported by NSF-STC `BioXFEL' (STC-1231306). E. A. Stojkovic was supported by NSF RUI grant BIO-MCB 1413360 and NIH grant T34 GM105549-01 NU-STARS. K. Moffat was supported by NIH grant EY024363. S. Westenhoff acknowledges support by the European Research Council, contract number 279944. The Academy of Finland is acknowledged for grants 296135 (J. Ihalainen) and 285461 (H. Takala). P. Fromme and S. Roy-Chowdhuri also acknowledge support from the NIH Femtosecond Nano-crystallography of Membrane Proteins (No. R01GM095583). J. Ihalainen and S. Westenhoff acknowledge support by the Swedish Foundation for International Cooperation in Research and Higher Education. ...
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