3HJI

1.8 Angstrom Crystal Structure of the I74V:I85V Variant of Vivid (VVD).

3HJI の概要

• エントリーDOI: 10.2210/pdb3hji/pdb
• 関連するPDBエントリー: 2pd7 2pd8 2pdr 2pdT 3d72 3HJK
• 分子名称: Vivid PAS protein VVD, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• 機能のキーワード: photoreceptor, circadian clock, lov, fad, signaling protein
• 由来する生物種: Neurospora crassa
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 36541.00

構造登録者

Zoltowski, B.D.,Vaccaro, B.J.,Crane, B.R. (登録日: 2009-05-21, 公開日: 2009-09-29, 最終更新日: 2023-09-06)

主引用文献

Zoltowski, B.D.,Vaccaro, B.,Crane, B.R.
Mechanism-based tuning of a LOV domain photoreceptor.
Nat.Chem.Biol., 5:827-834, 2009

PubMed Abstract: Phototropin-like LOV domains form a cysteinyl-flavin adduct in response to blue light but show considerable variation in output signal and the lifetime of the photo-adduct signaling state. Mechanistic studies of the slow-cycling fungal LOV photoreceptor Vivid (VVD) reveal the importance of reactive cysteine conformation, flavin electronic environment and solvent accessibility for adduct scission and thermal reversion. Proton inventory, pH effects, base catalysis and structural studies implicate flavin N(5) deprotonation as rate-determining for recovery. Substitutions of active site residues Ile74, Ile85, Met135 and Met165 alter photoadduct lifetimes by over four orders of magnitude in VVD, and similar changes in other LOV proteins show analogous effects. Adduct state decay rates also correlate with changes in conformational and oligomeric properties of the protein necessary for signaling. These findings link natural sequence variation of LOV domains to function and provide a means to design broadly reactive light-sensitive probes.

PubMed: 19718042
DOI: 10.1038/nchembio.210

実験手法

X-RAY DIFFRACTION (1.8 Å)