Detail Conformational Switching in the Fungal Light Sensor Vivid   Oleh:  Zoltowski, Brian D. ; Schwerdtfeger, Carsten ; Widom, Joanne ; Loros, Jennifer J. ; Bilwes, Alexandrine M. ; Dunlap, Jay C. ; Crane, Brian R Jenis: Article from Bulletin/Magazine Dalam koleksi: SCIENCE (keterangan: ada di Proquest) vol. 316 no. 5827 (May 2007), page 1054. Topik: Biochemistry Ketersediaan Perpustakaan FK Nomor Panggil: S01.K.2007.05 Non-tandon: 1 (dapat dipinjam: 0) Tandon: tidak ada     Lihat Detail Induk Isi artikel 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-l, ZEITLUPE, ENVOY, and flavin-binding, kelch repeat, F-BOX 1 (FKF1). Opini Anda Klik untuk menuliskan opini Anda tentang koleksi ini! Kembali

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