Lit-state solution structure of EL222 in complex with DNA
The transcription factor EL222 regulates gene expression in a light-dependent manner and, as a consequence, has found widespread use in optogenetic applications to control gene expression patterns in vivo. At the molecular level, the protein displays a simple architecture consisting of a flavin-binding light-oxygen-voltage (LOV) domain and a DNA-binding helix-turn-helix (HTH) module. The crystal structure of dark-adapted EL222 shows that LOV and HTH domains are tightly packed against each other thereby blocking the recognition of DNA. Upon excitation of the flavin moiety with blue light, EL222 undergoes conformational changes that lead to its association with DNA. However, our knowledge of the light-adapted states remains incomplete. We propose to employ an integrative structural biology approach including small-angle scattering techniques, SAXS and SANS, among others in order to model the solution structure of EL222/DNA complexes. The gathered information is expected to shed light on the signal transduction mechanism of LOV photoreceptors and might help in the design of photocontrolled protein-DNA interactions.
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The recommended format for citing this dataset in a research publication is in the following format:
Gustavo Fuertes; CHAUDHARI Aditya and MARTEL Anne. (2021). Lit-state solution structure of EL222 in complex with DNA. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-03-1045
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