Tuning flavin environment to detect and control light-induced conformational switching in Drosophila cryptochrome

Chandrasekaran et al. engineered the Drosophila circadian clock protein Cryptochrome (dCRY) to form the neutral semiquinone, which serves as a dark-state proxy. They find that the C-terminal tail of dCRY remains docked when the flavin ring is reduced but uncharged. dCRY His378 variants provide insig...

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Autores principales:	Siddarth Chandrasekaran, Connor M. Schneps, Robert Dunleavy, Changfan Lin, Cristina C. DeOliveira, Abir Ganguly, Brian R. Crane
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/239433bfd7aa4c559db2c188b3ff245d
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spelling	oai:doaj.org-article:239433bfd7aa4c559db2c188b3ff245d2021-12-02T15:52:46ZTuning flavin environment to detect and control light-induced conformational switching in Drosophila cryptochrome10.1038/s42003-021-01766-22399-3642https://doaj.org/article/239433bfd7aa4c559db2c188b3ff245d2021-02-01T00:00:00Zhttps://doi.org/10.1038/s42003-021-01766-2https://doaj.org/toc/2399-3642Chandrasekaran et al. engineered the Drosophila circadian clock protein Cryptochrome (dCRY) to form the neutral semiquinone, which serves as a dark-state proxy. They find that the C-terminal tail of dCRY remains docked when the flavin ring is reduced but uncharged. dCRY His378 variants provide insights into the recognition motifs for dCRY turnover and strategies for optogenetic tools.Siddarth ChandrasekaranConnor M. SchnepsRobert DunleavyChangfan LinCristina C. DeOliveiraAbir GangulyBrian R. CraneNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 4, Iss 1, Pp 1-12 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Siddarth Chandrasekaran Connor M. Schneps Robert Dunleavy Changfan Lin Cristina C. DeOliveira Abir Ganguly Brian R. Crane Tuning flavin environment to detect and control light-induced conformational switching in Drosophila cryptochrome
description	Chandrasekaran et al. engineered the Drosophila circadian clock protein Cryptochrome (dCRY) to form the neutral semiquinone, which serves as a dark-state proxy. They find that the C-terminal tail of dCRY remains docked when the flavin ring is reduced but uncharged. dCRY His378 variants provide insights into the recognition motifs for dCRY turnover and strategies for optogenetic tools.
format	article
author	Siddarth Chandrasekaran Connor M. Schneps Robert Dunleavy Changfan Lin Cristina C. DeOliveira Abir Ganguly Brian R. Crane
author_facet	Siddarth Chandrasekaran Connor M. Schneps Robert Dunleavy Changfan Lin Cristina C. DeOliveira Abir Ganguly Brian R. Crane
author_sort	Siddarth Chandrasekaran
title	Tuning flavin environment to detect and control light-induced conformational switching in Drosophila cryptochrome
title_short	Tuning flavin environment to detect and control light-induced conformational switching in Drosophila cryptochrome
title_full	Tuning flavin environment to detect and control light-induced conformational switching in Drosophila cryptochrome
title_fullStr	Tuning flavin environment to detect and control light-induced conformational switching in Drosophila cryptochrome
title_full_unstemmed	Tuning flavin environment to detect and control light-induced conformational switching in Drosophila cryptochrome
title_sort	tuning flavin environment to detect and control light-induced conformational switching in drosophila cryptochrome
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/239433bfd7aa4c559db2c188b3ff245d
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Tuning flavin environment to detect and control light-induced conformational switching in Drosophila cryptochrome

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