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 accessAbstract
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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Cites
[20] Processing of X-ray diffraction data collected in oscillation mode
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Analysis of the genome sequence of the flowering plant Arabidopsis thaliana
Initiative, T. A. G. (2000) · Nature · doi:10.1038/35048692 · Cited by 9,301
phot1 and phot2 mediate blue light regulation of stomatal opening
Kinoshita, T., Doi, M., Suetsugu, N., Kagawa, T., Wada, M., & Shimazaki, K.-I. (2001) · Nature · doi:10.1038/414656a · Cited by 899 · cited 2×
“, 1998), and control phototropism, light-induced chloroplast movement, and stomatal opening (Huala et al., 1997; Christie et al., 1998; Jarillo et al., 2001; Kagawa et al., 2001; Kinoshita et al., 2001).”
BackgroundArabidopsis NPL1: A Phototropin Homolog Controlling the Chloroplast High-Light Avoidance Response
Kagawa, T., Sakai, T., Suetsugu, N., Oikawa, K., Ishiguro, S., Kato, T., Tabata, S., Okada, K., & Wada, M. (2001) · Science · doi:10.1126/science.291.5511.2138 · Cited by 651
Phototropin-related NPL1 controls chloroplast relocation induced by blue light
Jarillo, J. A., Gabrys, H., Capel, J., Alonso, J. M., Ecker, J. R., & Cashmore, A. R. (2001) · Nature · doi:10.1038/35073622 · Cited by 476
Arabidopsis NPH3: A NPH1 Photoreceptor-Interacting Protein Essential for Phototropism
Motchoulski, A., & Liscum, E. (1999) · Science · doi:10.1126/science.286.5441.961 · Cited by 320
Sato, Y., Wada, M., & Kadota, A. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.2.269 · Cited by 148
Cited by
Phototropin Blue-Light Receptors
Christie, J. M. (2007) · Annual Review of Plant Biology · doi:10.1146/annurev.arplant.58.032806.103951 · Cited by 937
Phototropins 1 and 2: versatile plant blue-light receptors
Briggs, W. R., & Christie, J. M. (2002) · Trends in Plant Science · doi:10.1016/s1360-1385(02)02245-8 · Cited by 785
Structure and Signaling Mechanism of Per-ARNT-Sim Domains
Möglich, A., Ayers, R. A., & Moffat, K. (2009) · Structure · doi:10.1016/j.str.2009.08.011 · Cited by 531
Self-citationStructure and function of plant photoreceptors
Möglich, A., Yang, X., Ayers, R. A., & Moffat, K. (2010) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-042809-112259 · Cited by 499
Self-citationStructural basis of ultraviolet-B perception by UVR8
Wu, D., Hu, Q., Yan, Z., Chen, W., Yan, C., Huang, X., Zhang, J., Yang, P., Deng, H., Wang, J., et al. (2012) · Nature · doi:10.1038/nature10931 · Cited by 431
Metadata
- Authors
- Crosson, S., & Moffat, K.
- Venue
- The Plant Cell
- Publisher
- Oxford University Press (OUP)
- 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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