Summary for 6CNY
Entry DOI | 10.2210/pdb6cny/pdb |
Related | 2PD7 2PD8 2PDR |
Descriptor | Vivid PAS protein VVD, FLAVIN MONONUCLEOTIDE (3 entities in total) |
Functional Keywords | lov domain; flavin; photoreceptor; circadian clock, circadian clock protein |
Biological source | Neurospora crassa |
Total number of polymer chains | 4 |
Total formula weight | 70812.29 |
Authors | Zoltowski, B.D.,Shabalin, I.G.,Kowiel, M.,Porebski, P.J.,Crane, B.R.,Bilwes, A.M. (deposition date: 2018-03-09, release date: 2018-03-21, Last modification date: 2023-10-04) |
Primary citation | Zoltowski, B.D.,Schwerdtfeger, C.,Widom, J.,Loros, J.J.,Bilwes, A.M.,Dunlap, J.C.,Crane, B.R. Conformational switching in the fungal light sensor Vivid. Science, 316:1054-1057, 2007 Cited by PubMed Abstract: The Neurospora crassa photoreceptor Vivid tunes blue-light responses and modulates gating of the circadian clock. Crystal structures of dark-state and light-state Vivid reveal a light, oxygen, or voltage Per-Arnt-Sim domain with an unusual N-terminal cap region and a loop insertion that accommodates the flavin cofactor. Photoinduced formation of a cystein-flavin adduct drives flavin protonation to induce an N-terminal conformational change. A cysteine-to-serine substitution remote from the flavin adenine dinucleotide binding site decouples conformational switching from the flavin photocycle and prevents Vivid from sending signals in Neurospora. Key elements of this activation mechanism are conserved by other photosensors such as White Collar-1, ZEITLUPE, ENVOY, and flavin-binding, kelch repeat, F-BOX 1 (FKF1). PubMed: 17510367DOI: 10.1126/science.1137128 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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