2LB5

Refined Structural Basis for the Photoconversion of A Phytochrome to the Activated FAR-RED LIGHT-ABSORBING Form

2LB5 の概要

• エントリーDOI: 10.2210/pdb2lb5/pdb
• 関連するPDBエントリー: 2LB9
• NMR情報: BMRB: 17546
• 分子名称: Sensor histidine kinase, PHYCOCYANOBILIN (2 entities in total)
• 機能のキーワード: pcb, kinase, transferase, gaf domain, phosphoprotein
• 由来する生物種: Synechococcus sp. JA-2-3B'a(2-13)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23928.22

構造登録者

Cornilescu, C.C.,Cornilescu, G.,Ulijasz, A.T.,Vierstra, R.D.,Markley, J.L. (登録日: 2011-03-23, 公開日: 2011-06-29, 最終更新日: 2024-10-30)

主引用文献

Ulijasz, A.T.,Cornilescu, G.,Cornilescu, C.C.,Zhang, J.,Rivera, M.,Markley, J.L.,Vierstra, R.D.
Structural basis for the photoconversion of a phytochrome to the activated Pfr form.
Nature, 463:250-254, 2010

PubMed Abstract: Phytochromes are a collection of bilin-containing photoreceptors that regulate numerous photoresponses in plants and microorganisms through their ability to photointerconvert between a red-light-absorbing, ground state (Pr) and a far-red-light-absorbing, photoactivated state (Pfr). Although the structures of several phytochromes as Pr have been determined, little is known about the structure of Pfr and how it initiates signalling. Here we describe the three-dimensional solution structure of the bilin-binding domain as Pfr, using the cyanobacterial phytochrome from Synechococcus OSB'. Contrary to predictions, light-induced rotation of the A pyrrole ring but not the D ring is the primary motion of the chromophore during photoconversion. Subsequent rearrangements within the protein then affect intradomain and interdomain contact sites within the phytochrome dimer. On the basis of our models, we propose that phytochromes act by propagating reversible light-driven conformational changes in the bilin to altered contacts between the adjacent output domains, which in most phytochromes direct differential phosphotransfer.

PubMed: 20075921
DOI: 10.1038/nature08671

実験手法

SOLUTION NMR