1N9O

Crystal structure of the Phot-LOV1 domain from Chlamydomonas reinhardtii in illuminated state. Composite data set.

1N9O の概要

• エントリーDOI: 10.2210/pdb1n9o/pdb
• 関連するPDBエントリー: 1G28 1JNU 1N9L 1N9N
• 分子名称: putative blue light receptor, SULFATE ION, FLAVIN MONONUCLEOTIDE, ... (4 entities in total)
• 機能のキーワード: phototropin, flavin, electron transport
• 由来する生物種: Chlamydomonas reinhardtii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12542.05

構造登録者

Fedorov, R.,Schlichting, I.,Hartmann, E.,Domratcheva, T.,Fuhrmann, M.,Hegemann, P. (登録日: 2002-11-25, 公開日: 2003-06-17, 最終更新日: 2024-11-20)

主引用文献

Fedorov, R.,Schlichting, I.,Hartmann, E.,Domratcheva, T.,Fuhrmann, M.,Hegemann, P.
Crystal structures and molecular mechanism of a light-induced signaling switch: The Phot-LOV1 domain from Chlamydomonas reinhardtii.
Biophys.J., 84:2474-2482, 2003

PubMed Abstract: Phot proteins (phototropins and homologs) are blue-light photoreceptors that control mechanical processes like phototropism, chloroplast relocation, or guard-cell opening in plants. Phot receptors consist of two flavin mononucleotide (FMN)-binding light, oxygen, or voltage (LOV) domains and a C-terminal serine/threonine kinase domain. We determined crystal structures of the LOV1 domain of Phot1 from the green alga Chlamydomonas reinhardtii in the dark and illuminated state to 1.9 A and 2.8 A resolution, respectively. The structure resembles that of LOV2 from Adiantum (Crosson, S. and K. Moffat. 2001. PROC: Natl. Acad. Sci. USA. 98:2995-3000). In the resting dark state of LOV1, the reactive Cys-57 is present in two conformations. Blue-light absorption causes formation of a proposed active signaling state that is characterized by a covalent bond between the flavin C4a and the thiol of Cys-57. There are differences around the FMN chromophore but no large overall conformational changes. Quantum chemical calculations based on the crystal structures revealed the electronic distribution in the active site during the photocycle. The results suggest trajectories for electrons, protons, and the active site cysteine and offer an interpretation of the reaction mechanism.

PubMed: 12668455
DOI: 10.1016/S0006-3495(03)75052-8

実験手法

X-RAY DIFFRACTION (2.8 Å)