3C2W

Crystal structure of the photosensory core domain of P. aeruginosa bacteriophytochrome PaBphP in the Pfr state

3C2W の概要

• エントリーDOI: 10.2210/pdb3c2w/pdb
• 分子名称: Bacteriophytochrome, BILIVERDINE IX ALPHA (3 entities in total)
• 機能のキーワード: knot structure, chromophore, kinase, phosphoprotein, photoreceptor protein, receptor, sensory transduction, transferase, signaling protein
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 459247.01

構造登録者

Yang, X.,Kuk, J.,Moffat, K. (登録日: 2008-01-25, 公開日: 2008-09-23, 最終更新日: 2024-10-30)

主引用文献

Yang, X.,Kuk, J.,Moffat, K.
Crystal structure of Pseudomonas aeruginosa bacteriophytochrome: photoconversion and signal transduction.
Proc.Natl.Acad.Sci.USA, 105:14715-14720, 2008

PubMed Abstract: Phytochromes are red-light photoreceptors that regulate light responses in plants, fungi, and bacteria via reversible photoconversion between red (Pr) and far-red (Pfr) light-absorbing states. Here we report the crystal structure at 2.9 A resolution of a bacteriophytochrome from Pseudomonas aeruginosa with an intact, fully photoactive photosensory core domain in its dark-adapted Pfr state. This structure reveals how unusual interdomain interactions, including a knot and an "arm" structure near the chromophore site, bring together the PAS (Per-ARNT-Sim), GAF (cGMP phosphodiesterase/adenyl cyclase/FhlA), and PHY (phytochrome) domains to achieve Pr/Pfr photoconversion. The PAS, GAF, and PHY domains have topologic elements in common and may have a single evolutionary origin. We identify key interactions that stabilize the chromophore in the Pfr state and provide structural and mutational evidence to support the essential role of the PHY domain in efficient Pr/Pfr photoconversion. We also identify a pair of conserved residues that may undergo concerted conformational changes during photoconversion. Modeling of the full-length bacteriophytochrome structure, including its output histidine kinase domain, suggests how local structural changes originating in the photosensory domain modulate interactions between long, cross-domain signaling helices at the dimer interface and are transmitted to the spatially distant effector domain, thereby regulating its histidine kinase activity.

PubMed: 18799746
DOI: 10.1073/pnas.0806718105

実験手法

X-RAY DIFFRACTION (2.9 Å)