Source:
Generated By: https://synbiohub.org/public/igem/igem2sbol/1
Created by: Johanna Chesnel
Date created: 2015-09-17 11:00:00
Date modified: 2015-09-18 02:54:35
VVD - homodimer photoreceptor
| Types | DnaRegion |
| Roles | CDS Coding |
| Sequences | BBa_K1616014_sequence (Version 1) |
Description
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; M??ller & 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 (M??ller & Weber, 2013; Nihongaki, Suzuki, Kawano, & Sato, 2014).