1ZTU

Structure of the chromophore binding domain of bacterial phytochrome

1ZTU の概要

• エントリーDOI: 10.2210/pdb1ztu/pdb
• 分子名称: Bacteriophytochrome, BILIVERDINE IX ALPHA (3 entities in total)
• 機能のキーワード: phytochrome, bacteriophytochrome, biliverdin ix, chromophore, pas, gaf, knot, transferase
• 由来する生物種: Deinococcus radiodurans
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37995.87

構造登録者

Wagner, J.R.,Brunzelle, J.S.,Forest, K.T.,Vierstra, R.D. (登録日: 2005-05-27, 公開日: 2005-11-15, 最終更新日: 2024-11-06)

主引用文献

Wagner, J.R.,Brunzelle, J.S.,Forest, K.T.,Vierstra, R.D.
A light-sensing knot revealed by the structure of the chromophore-binding domain of phytochrome.
Nature, 438:325-331, 2005

PubMed Abstract: Phytochromes are red/far-red light photoreceptors that direct photosensory responses across the bacterial, fungal and plant kingdoms. These include photosynthetic potential and pigmentation in bacteria as well as chloroplast development and photomorphogenesis in plants. Phytochromes consist of an amino-terminal region that covalently binds a single bilin chromophore, followed by a carboxy-terminal dimerization domain that often transmits the light signal through a histidine kinase relay. Here we describe the three-dimensional structure of the chromophore-binding domain of Deinococcus radiodurans phytochrome assembled with its chromophore biliverdin in the Pr ground state. Our model, refined to 2.5 A resolution, reaffirms Cys 24 as the chromophore attachment site, locates key amino acids that form a solvent-shielded bilin-binding pocket, and reveals an unusually formed deep trefoil knot that stabilizes this region. The structure provides the first three-dimensional glimpse into the photochromic behaviour of these photoreceptors and helps to explain the evolution of higher plant phytochromes from prokaryotic precursors.

PubMed: 16292304
DOI: 10.1038/nature04118

実験手法

X-RAY DIFFRACTION (2.5 Å)