Cited by 317Light effects on plantsPhotoreceptor and optogenetics researchPlant Molecular Biology Research

N- and C-Terminal Flanking Regions Modulate Light-Induced Signal Transduction in the LOV2 Domain of the Blue Light Sensor Phototropin 1 from Avena sativa ,

Halavaty, Andrei S., Moffat, Keith·2007·Biochemistry

Abstract

Light sensing by photoreceptors controls phototropism, chloroplast movement, stomatal opening, and leaf expansion in plants. Understanding the molecular mechanism by which these processes are regulated requires a quantitative description of photoreceptor dynamics. We focus on a light-driven signal transduction mechanism in the LOV2 domain (LOV, light, oxygen, voltage) of the blue light photoreceptor phototropin 1 from Avena sativa (oat). High-resolution crystal structures of the dark and light states of an oat LOV2 construct including residues Leu404 through Leu546 (LOV2 (404-546)) have been determined at 105 and 293 K. In all four structures, LOV2 (404-546) exhibits the typical Per-ARNT-Sim (PAS) fold, flanked by an additional conserved N-terminal turn-helix-turn motif and a C-terminal flanking region containing an amphipathic Jalpha helix. These regions dock on the LOV2 core domain and bury several hydrophobic residues of the central beta-sheet of the core domain that would otherwise be exposed to solvent. Light structures of LOV2 (404-546) reveal that formation of the covalent bond between Cys450 and the C4a atom of the flavin mononucleotide (FMN) results in local rearrangement of the hydrogen-bonding network in the FMN binding pocket. These rearrangements are associated with disruption of the Asn414-Asp515 hydrogen bond on the surface of the protein and displacement of the N- and C-terminal flanking regions of LOV2 (404-546), both of which constitute a structural signal.

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Crossref · 10.1021/bi701543e

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  • Blue light induces conformational changes in LOV2 to enhance STK phosphorylation.

    “Through high-resolution crystal structure analysis and spectroscopic measurements, blue light was found to induce conformational changes in the LOV2 to enhance STK phosphorylation (Iwata et al., 2003; Halavaty and Moffat, 2007; Liscum et al., 2014).”

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Authors
Halavaty, A. S., & Moffat, K.
Affiliations
University of Chicago (US)
Corresponding author
Moffat, Keith
Venue
Biochemistry
Published
2007-11-15
Volume
46
Issue
49
Pages
14001-14009
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
OpenAlex
W2096165020
Cited by
317
References
50
Citations by year
2026: 14 · 2025: 11 · 2024: 16 · 2023: 28 · 2022: 12 · 2021: 22 · 2020: 27 · 2019: 19 · 2018: 9 · 2017: 10 · 2016: 13 · 2015: 18 · 2014: 19 · 2013: 20 · 2012: 22
FWCI
15.76
Type
journal article
Language
en
Open access
closed
Locations
  • Biochemistry (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Institute of General Medical Sciences (GM 036452)
  • National Center for Research Resources (RR07 707)
Topics
  • Life Sciences › Agricultural and Biological Sciences › Plant Science › Light effects on plants
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Photoreceptor and optogenetics research
  • Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
Keywords
phototropin 1, LOV2 domain, blue-light photoreceptor, Avena sativa, flavin mononucleotide, hydrogen bond network, protein crystal structure, light-induced conformational change, phototropism
MeSH terms
Amino Acid Sequence, Darkness, Flavoproteins, Light, Models, Molecular, Molecular Sequence Data, Signal Transduction, Sequence Alignment, Protein Structure, Tertiary, Crystallography, X-Ray, Avena, Photosynthetic Reaction Center Complex Proteins, Cryptochromes

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