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Cited by 357

The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.

Photoexcited Structure of a Plant Photoreceptor Domain Reveals a Light-Driven Molecular Switch

Open access
Crosson, Sean, Moffat, Keith·2002·The Plant Cell

Abstract

The phototropins are flavoprotein kinases that control phototropic bending, light-induced chloroplast movement, and stomatal opening in plants. Two flavin mononucleotide binding light, oxygen, or voltage (LOV) domains are the sites for initial photochemistry in these blue light photoreceptors. We have determined the steady state, photoexcited crystal structure of a flavin-bound LOV domain. The structure reveals a unique photochemical switch in the flavin binding pocket in which the absorption of light drives the formation of a reversible covalent bond between a highly conserved Cys residue and the flavin cofactor. This provides a molecular picture of a cysteinyl-flavin covalent adduct, the presumed signaling species that leads to phototropin kinase activation and subsequent signal transduction. We identify closely related LOV domains in two eubacterial proteins that suggests the light-induced conformational change evident in this structure is an ancient biomolecular response to light, arising before the appearance of plants.

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Metadata

Authors
Crosson, S., & Moffat, K.
Venue
The Plant Cell
Published
2002-04-29
Volume
14
Issue
5
Pages
1067-1075
ISSN
  • 1040-4651 (ISSN-L)
  • 1532-298X
OpenAlex
W2110075655
Cited by
357
References
7
FWCI
31.49
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Photoexcited Structure of a Plant Photoreceptor Domain Reveals a Light-Driven Molecular Switch. https://app.cochat.ai/papers/10.1105/tpc.010475
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Crosson, S., & Moffat, K. (2002). Photoexcited Structure of a Plant Photoreceptor Domain Reveals a Light-Driven Molecular Switch. The Plant Cell. https://doi.org/10.1105/tpc.010475

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