3RH8

Crystal Structure of the Light-state Dimer of Fungal Blue-Light Photoreceptor Vivid

3RH8 の概要

• エントリーDOI: 10.2210/pdb3rh8/pdb
• 関連するPDBエントリー: 2PD7 2PD8 2PDR 2PDT
• 分子名称: Vivid PAS protein VVD, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• 機能のキーワード: light-state dimer, photoreceptor, lov pas domain, circadian clock protein, blue-light sensing, transcription inhibitor
• 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: 35237.58

構造登録者

Vaidya, A.T.,Crane, B.R. (登録日: 2011-04-11, 公開日: 2011-09-21, 最終更新日: 2024-11-20)

主引用文献

Vaidya, A.T.,Chen, C.H.,Dunlap, J.C.,Loros, J.J.,Crane, B.R.
Structure of a Light-Activated LOV Protein Dimer That Regulates Transcription.
Sci.Signal., 4:ra50-ra50, 2011

PubMed Abstract: Light, oxygen, or voltage (LOV) protein domains are present in many signaling proteins in bacteria, archaea, protists, plants, and fungi. The LOV protein VIVID (VVD) of the filamentous fungus Neurospora crassa enables the organism to adapt to constant or increasing amounts of light and facilitates proper entrainment of circadian rhythms. Here, we determined the crystal structure of the fully light-adapted VVD dimer and reveal the mechanism by which light-driven conformational change alters the oligomeric state of the protein. Light-induced formation of a cysteinyl-flavin adduct generated a new hydrogen bond network that released the amino (N) terminus from the protein core and restructured an acceptor pocket for binding of the N terminus on the opposite subunit of the dimer. Substitution of residues critical for the switch between the monomeric and the dimeric states of the protein had profound effects on light adaptation in Neurospora. The mechanism of dimerization of VVD provides molecular details that explain how members of a large family of photoreceptors convert light responses to alterations in protein-protein interactions.

PubMed: 21868352
DOI: 10.1126/scisignal.2001945

実験手法

X-RAY DIFFRACTION (2.75 Å)