5L8M
Wild-type PAS-GAF fragment from Deinococcus radiodurans Bphp collected at LCLS
5L8M の概要
| エントリーDOI | 10.2210/pdb5l8m/pdb |
| 関連するPDBエントリー | 5K5B |
| 分子名称 | Bacteriophytochrome, 3-[2-[(Z)-[3-(2-carboxyethyl)-5-[(Z)-(4-ethenyl-3-methyl-5-oxidanylidene-pyrrol-2-ylidene)methyl]-4-methyl-pyrrol-1-ium -2-ylidene]methyl]-5-[(Z)-[(3E)-3-ethylidene-4-methyl-5-oxidanylidene-pyrrolidin-2-ylidene]methyl]-4-methyl-1H-pyrrol-3- yl]propanoic acid, ACETATE ION, ... (4 entities in total) |
| 機能のキーワード | kinase, photosensor, transferase, phytochrome |
| 由来する生物種 | Deinococcus radiodurans |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 37874.17 |
| 構造登録者 | Claesson, E.,Takala, H.,Edlund, P.,Henry, L.,Dods, R.,Schmidt, M.,Westenhoff, S. (登録日: 2016-06-08, 公開日: 2016-10-26, 最終更新日: 2024-11-13) |
| 主引用文献 | Edlund, P.,Takala, H.,Claesson, E.,Henry, L.,Dods, R.,Lehtivuori, H.,Panman, M.,Pande, K.,White, T.,Nakane, T.,Berntsson, O.,Gustavsson, E.,Bath, P.,Modi, V.,Roy-Chowdhury, S.,Zook, J.,Berntsen, P.,Pandey, S.,Poudyal, I.,Tenboer, J.,Kupitz, C.,Barty, A.,Fromme, P.,Koralek, J.D.,Tanaka, T.,Spence, J.,Liang, M.,Hunter, M.S.,Boutet, S.,Nango, E.,Moffat, K.,Groenhof, G.,Ihalainen, J.,Stojkovic, E.A.,Schmidt, M.,Westenhoff, S. The room temperature crystal structure of a bacterial phytochrome determined by serial femtosecond crystallography. Sci Rep, 6:35279-35279, 2016 Cited by PubMed Abstract: 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 chromophore-binding domains of the Deinococcus radiodurans phytochrome at 2.1 Å 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 1.35 Å 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. PubMed: 27756898DOI: 10.1038/srep35279 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.1 Å) |
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