Difference between revisions of "Part:BBa K1616014"

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VVD - homodimer photoreceptor

Among other photoreceptors, Vivid (VVD) is the smallest known Light–oxygen–voltage (LOV) domain protein and photo-inducible dimer. Isolated from Neurospora crassa, VVD forms a homo-dimer in response to a blue-light stimulus. The LOV domain, present in VVD, is a small blue-light sensing domain found in prokaryotes, fungi and plants. After blue-light activation, a covalent bond is formed between the co-factor Flavin mononucleotide (FMN) and one of the cysteine residue. This bond leads to a conformational change inducing functions by dissociating the C-terminal a-helix (Ja) and the LOV-core. In VVD, this undock triggers homodimerization (Bilwes, Dunlap, & Crane, 2007; Müller & Weber, 2013).

Contrary to other photoreceptors, VVD is a small protein with 150 amino-acids facilitating accurate molecular design and avoiding steric issues. Moreover, it is a homo-dimer when most of photo-inducible dimers are heterodimers. In addition, the use of VVD is easy; and doesn’t need any addition of co-factors: VVD works with Flavin adenine dinucleotide (FAD) which is already abundant in eukaryote and prokaryote cells (Müller & Weber, 2013; Nihongaki, Suzuki, Kawano, & Sato, 2014).

Crystal structure of the Lightstate Dimer of fungal Blue-light Photoreceptor Vivid (VVD) (Reference RSCB-PDB: 3RH8)

Design Notes

We found illegal sites (PstI) into VVD sequence, those one have been removed.

Source

VVD was isolated from Neurospora crassa.

References

Bilwes, A. M., Dunlap, J. C., & Crane, B. R. (2007). Conformational Switching in the Fungal Light Sensor Vivid, 36(May), 1054–1058. Müller, K., & Weber, W. (2013). Optogenetic tools for mammalian systems. Molecular bioSystems, 9(4), 596–608. http://doi.org/10.1039/c3mb25590e