5XT2

Crystal structures of full-length FixJ from B. japonicum crystallized in space group P212121

5XT2 の概要

• エントリーDOI: 10.2210/pdb5xt2/pdb
• 関連するPDBエントリー: 5XSO
• 分子名称: Response regulator FixJ, MAGNESIUM ION, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: response regulater, fixj/narl family, dna binding protein, full-length, unphosphorylated monomeric state
• 由来する生物種: Bradyrhizobium japonicum
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 117959.60

構造登録者

Nishizono, Y.,Hisano, T.,Shiro, Y.,Sawai, H.,Wright, G.S.A.,Saeki, A.,Hikima, T.,Nakamura, H.,Yamamoto, M.,Antonyuk, S.V.,Hasnain, S.S. (登録日: 2017-06-16, 公開日: 2018-05-23, 最終更新日: 2024-03-27)

主引用文献

Wright, G.S.A.,Saeki, A.,Hikima, T.,Nishizono, Y.,Hisano, T.,Kamaya, M.,Nukina, K.,Nishitani, H.,Nakamura, H.,Yamamoto, M.,Antonyuk, S.V.,Hasnain, S.S.,Shiro, Y.,Sawai, H.
Architecture of the complete oxygen-sensing FixL-FixJ two-component signal transduction system.
Sci Signal, 11:-, 2018

PubMed Abstract: The symbiotic nitrogen-fixing bacterium is critical to the agro-industrial production of soybean because it enables the production of high yields of soybeans with little use of nitrogenous fertilizers. The FixL and FixJ two-component system (TCS) of this bacterium ensures that nitrogen fixation is only stimulated under conditions of low oxygen. When it is not bound to oxygen, the histidine kinase FixL undergoes autophosphorylation and transfers phosphate from adenosine triphosphate (ATP) to the response regulator FixJ, which, in turn, stimulates the expression of genes required for nitrogen fixation. We purified full-length FixL and FixJ proteins and defined their structures individually and in complex using small-angle x-ray scattering, crystallographic, and in silico modeling techniques. Comparison of active and inactive forms of FixL suggests that intramolecular signal transduction is driven by local changes in the sensor domain and in the coiled-coil region connecting the sensor and histidine kinase domains. We also found that FixJ exhibits conformational plasticity not only in the monomeric state but also in tetrameric complexes with FixL during phosphotransfer. This structural characterization of a complete TCS contributes both a mechanistic and evolutionary understanding to TCS signal relay, specifically in the context of the control of nitrogen fixation in root nodules.

PubMed: 29636388
DOI: 10.1126/scisignal.aaq0825

実験手法

X-RAY DIFFRACTION (2.652 Å)