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  Crystal structures and molecular mechanism of a light-induced signaling switch: The Phot-LOV1 domain from Chlamydomonas reinhardtii

Fedorov, R., Schlichting, I., Hartmann, E., Domratcheva, T., Fuhrmann, M., & Hegemann, P. (2003). Crystal structures and molecular mechanism of a light-induced signaling switch: The Phot-LOV1 domain from Chlamydomonas reinhardtii. Biophysical Journal, 84(4), 2474-2482. doi:10.1016/S0006-3495(03)75052-8.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-B280-8 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-B281-6
Genre: Journal Article
Alternative Title : Crystal structures and molecular mechanism of a light-induced signaling switch: The Phot-LOV1 domain from Chlamydomonas reinhardtii

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 Creators:
Fedorov, Roman1, Author              
Schlichting, Ilme1, Author              
Hartmann, Elisabeth1, Author              
Domratcheva, Tatiana1, Author              
Fuhrmann, Markus, Author
Hegemann, Peter, Author
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1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 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.

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Language(s): eng - English
 Dates: 2002-07-112002-11-182003-04-01
 Publication Status: Published in print
 Pages: 9
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 Table of Contents: -
 Rev. Type: Peer
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Title: Biophysical Journal
  Other : Biophys. J.
Source Genre: Journal
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Publ. Info: Cambridge, Mass. : Cell Press
Pages: - Volume / Issue: 84 (4) Sequence Number: - Start / End Page: 2474 - 2482 Identifier: Other: 0006-3495
CoNE: https://pure.mpg.de/cone/journals/resource/954925385117