8F71

Crystal structure of the histidine kinase domain of bacteriophytochrome RpBphP2

8F71 の概要

• エントリーDOI: 10.2210/pdb8f71/pdb
• 分子名称: Histidine kinase, ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: histidine kinase, bacteriophytochrome, signaling protein, transferase
• 由来する生物種: Rhodopseudomonas palustris CGA009
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 60184.71

構造登録者

Yang, X.,Kumarapperuma, I.,Tom, I. (登録日: 2022-11-17, 公開日: 2023-11-22, 最終更新日: 2024-10-23)

主引用文献

Kumarapperuma, I.,Tom, I.P.,Bandara, S.,Montano, S.,Yang, X.
Mode of autophosphorylation in bacteriophytochromes RpBphP2 and RpBphP3.
Photochem Photobiol Sci, 22:1257-1266, 2023

PubMed Abstract: Phytochromes are red-light photoreceptors that regulate a wide range of physiological processes in plants, fungi and bacteria. Canonical bacteriophytochromes are photosensory histidine kinases that undergo light-dependent autophosphorylation, thereby regulating cellular responses to red light via two-component signaling pathways. However, the molecular mechanism of kinase activation remains elusive for bacteriophytochromes. In particular, the directionality of autophosphorylation is still an open question in these dimeric photoreceptor kinases. In this work, we perform histidine kinase assays on two tandem bacteriophytochromes RpBphP2 and RpBphP3 from the photosynthetic bacterium Rhodopseudomonas palustris. By examining the kinase activities of full-length bacteriophytochromes and two loss-of-function mutants under different light conditions, we demonstrate that RpBphP2 and RpBphP3 undergo light-dependent trans-phosphorylation between protomers in both homodimeric and heterodimeric forms. We have further determined the crystal structure of the histidine kinase domains of RpBphP2 at 3.19 Å resolution. Based on structural comparisons and homology modeling, we also present a model to account for the actions of trans-autophosphorylation in bacteriophytochromes.

PubMed: 36757561
DOI: 10.1007/s43630-023-00366-9

実験手法

X-RAY DIFFRACTION (3.19 Å)