1D7E
CRYSTAL STRUCTURE OF THE P65 CRYSTAL FORM OF PHOTOACTIVE YELLOW PROTEIN
1D7E の概要
| エントリーDOI | 10.2210/pdb1d7e/pdb |
| 関連するPDBエントリー | 2PHY |
| 分子名称 | PHOTOACTIVE YELLOW PROTEIN, 4'-HYDROXYCINNAMIC ACID (3 entities in total) |
| 機能のキーワード | photoreceptor, photosynthesis |
| 由来する生物種 | Halorhodospira halophila |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 13654.28 |
| 構造登録者 | Van Aalten, D.M.F.,Crielaard, W.,Hellingwerf, K.J.,Joshua-Tor, L. (登録日: 1999-10-17, 公開日: 2000-03-31, 最終更新日: 2025-03-26) |
| 主引用文献 | van Aalten, D.M.,Crielaard, W.,Hellingwerf, K.J.,Joshua-Tor, L. Conformational substates in different crystal forms of the photoactive yellow protein--correlation with theoretical and experimental flexibility. Protein Sci., 9:64-72, 2000 Cited by PubMed Abstract: The conformational changes during the photocycle of the photoactive yellow protein have been the subject of many recent studies. Spectroscopic measurements have shown that the photocycle also occurs in a crystalline environment, and this has been the basis for subsequent Laue diffraction and cryocrystallographic studies. These studies have shown that conformational changes during the photocycle are limited to the chromophore and its immediate environment. However, spectroscopic studies suggest the presence of large conformational changes in the protein. Here, we address this apparent discrepancy in two ways. First, we obtain a description of large concerted motions in the ground state of the yellow protein from NMR data and theoretical calculations. Second, we describe the high-resolution structure of the yellow protein crystallized in a different space group. The structure of the yellow protein differs significantly between the two crystal forms. We show that these differences can be used to obtain a description of the flexibility of the protein that is consistent with the motions observed in solution. PubMed: 10739248主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.39 Å) |
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