The room temperature crystal structure of a bacterial phytochrome determined by serial femtosecond crystallography
Edlund, P., Takala, H., Claesson, E., Henry, L., Dods, R., Lehtivuori, H., Panman, M., Pande, K., White, T., Nakane, T., Berntsson, O., Gustavsson, E., Båth, P., Modi, V., Roy-Chowdhury, S., Zook, J., Berntsen, P., Pandey, S., Poudyal, I., . . . Westenhoff, S. (2016). The room temperature crystal structure of a bacterial phytochrome determined by serial femtosecond crystallography. Scientific Reports, 6, 35279. https://doi.org/10.1038/srep35279
Julkaistu sarjassa
Scientific ReportsTekijät
Päivämäärä
2016Oppiaine
Solu- ja molekyylibiologiaFysikaalinen kemiaNanoscience CenterCell and Molecular BiologyPhysical ChemistryNanoscience CenterTekijänoikeudet
© the Authors, 2016. This is an open access article distributed under a Creative Commons Attribution 4.0 International License.
Phytochromes are a family of photoreceptors that control light responses of plants, fungi and bacteria.
A sequence of structural changes, which is not yet fully understood, leads to activation of an output
domain. Time-resolved serial femtosecond crystallography (SFX) can potentially shine light on these
conformational changes. Here we report the room temperature crystal structure of the chromophorebinding
domains of the Deinococcus radiodurans phytochrome at 2.1Å resolution.The structure was
obtained by serial femtosecond X-ray crystallography from microcrystals at an X-ray free electron
laser.We find overall good agreement compared to a crystal structure at 1.35Å resolution derived from
conventional crystallography at cryogenic temperatures, which we also report here. The thioether
linkage between chromophore and protein is subject to positional ambiguity at the synchrotron, but
is fully resolved with SFX. The study paves the way for time-resolved structural investigations of the
phytochrome photocycle with time-resolved SFX.
...
Julkaisija
Nature Publishing GroupISSN Hae Julkaisufoorumista
2045-2322Julkaisu tutkimustietojärjestelmässä
https://converis.jyu.fi/converis/portal/detail/Publication/26282980
Metadata
Näytä kaikki kuvailutiedotKokoelmat
Lisenssi
Ellei muuten mainita, aineiston lisenssi on © the Authors, 2016. This is an open access article distributed under a Creative Commons Attribution 4.0 International License.
Samankaltainen aineisto
Näytetään aineistoja, joilla on samankaltainen nimeke tai asiasanat.
-
The three-dimensional structure of Drosophila melanogaster (6–4) photolyase at room temperature
Cellini, Andrea; Wahlgren, Weixiao Yuan; Henry, Léocadie; Pandey, Suraj; Ghosh, Swagatha; Castillon, Leticia; Claesson, Elin; Takala, Heikki; Kübel, Joachim; Nimmrich, Amke; Kuznetsova, Valentyna; Nango, Eriko; Iwata, So; Owada, Shigeki; Stojković, Emina A.; Schmidt, Marius; Ihalainen, Janne A.; Westenhoff, Sebastian (Wiley-Blackwell, 2021)(6–4) photolyases are flavoproteins that belong to the photolyase/cryptochrome family. Their function is to repair DNA lesions using visible light. Here, crystal structures of Drosophila melanogaster (6–4) photolyase ... -
The primary structural photoresponse of phytochrome proteins captured by a femtosecond X-ray laser
Claesson, Elin; Wahlgren, Weixiao Yuan; Takala, Heikki; Pandey, Suraj; Castillon, Leticia; Kuznetsova, Valentyna; Henry, Léocadie; Panman, Matthijs; Carrillo, Melissa; Kübel, Joachim; Nanekar, Rahul; Isaksson, Linnéa; Nimmrich, Amke; Cellini, Andrea; Morozov, Dmitry; Maj, Michał; Kurttila, Moona; Bosman, Robert; Nango, Eriko; Tanaka, Rie; Tanaka, Tomoyuki; Fangjia, Luo; Iwata, So; Owada, Shigeki; Moffat, Keith; Groenhof, Gerrit; Stojkovic, Emina A.; Ihalainen, Janne A.; Schmidt, Marius; Westenhof, Sebastian (eLife Sciences Publications, 2020)Phytochrome proteins control the growth, reproduction, and photosynthesis of plants, fungi, and bacteria. Light is detected by a bilin cofactor, but it remains elusive how this leads to activation of the protein through ... -
Conserved histidine and tyrosine determine spectral responses through the water network in Deinococcus radiodurans phytochrome
Lehtivuori, Heli; Rumfeldt, Jessica; Mustalahti, Satu; Kurkinen, Sami; Takala, Heikki (Springer Science and Business Media LLC, 2022)Phytochromes are red light-sensing photoreceptor proteins that bind a bilin chromophore. Here, we investigate the role of a conserved histidine (H260) and tyrosine (Y263) in the chromophore-binding domain (CBD) of Deinococcus ... -
Structural analysis of two foldamer-type oligoamides – the effect of hydrogen bonding on solvate formation, crystal structures and molecular conformation
Suhonen, Aku; Nauha, Elisa; Salorinne, Kirsi; Helttunen, Kaisa; Nissinen, Maija (RSC Publishing, 2012)The crystal structures and molecular conformations of two foldamer-type oligoamides were analyzed. One polymorphic form and seven solvates were found for N¹,N³-bis(2-benzamidophenyl)benzene-1,3-dicarboxamide (the benzene ... -
Structural basis for light control of cell development revealed by crystal structures of a myxobacterial phytochrome
Woitowich, Nicole C.; Halavaty, Andrei S.; Waltz, Patricia; Kupitz, Christopher; Valera, Joseph; Tracy, Gregory; Gallagher, Kevin D.; Claesson, Elin; Nakane, Takanori; Pandey, Suraj; Nelson, Garrett; Tanaka, Rie; Nango, Eriko; Mizohata, Eiichi; Owada, Shigeki; Tono, Kensure; Joti, Yasumasa; Nugent, Angela C.; Patel, Hardik; Mapara, Ayesha; Hopkins, James; Duong, Phu; Bizhga, Dorina; Kovaleva, Svetlana E.; Peter, Rachael St.; Hernandez, Cynthia N.; Ozarowski, Wesley B.; Roy-Chowdhuri, Shatabdi; Yang, Jay-How; Edlund, Petra; Takala, Heikki; Ihalainen, Janne; Brayshaw, Jennifer; Norwood, Tyler; Poudyal, Ishwor; Fromme, Petra; Spence, John C. H.; Moffat, Keith; Westenhoff, Sebastian; Schmidt, Marius; Stojković, Emina A. (International Union of Crystallography, 2018)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 ...
Ellei toisin mainittu, julkisesti saatavilla olevia JYX-metatietoja (poislukien tiivistelmät) saa vapaasti uudelleenkäyttää CC0-lisenssillä.