1DRM

CRYSTAL STRUCTURE OF THE LIGAND FREE BJFIXL HEME DOMAIN

「1BV6」から置き換えられました

1DRM の概要

• エントリーDOI: 10.2210/pdb1drm/pdb
• 関連するPDBエントリー: 1BV5 1BV6 1DP6 1DP8 1DP9
• 分子名称: SENSOR PROTEIN FIXL, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• 機能のキーワード: fixl, heme domain, pas family, two-component system, histidine kinase, transferase
• 由来する生物種: Bradyrhizobium japonicum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15536.34

構造登録者

Gong, W.,Hao, B.,Mansy, S.S.,Gonzalez, G.,Gilles-Gonzalez, M.A.,Chan, M.K. (登録日: 2000-01-06, 公開日: 2000-01-24, 最終更新日: 2024-02-07)

主引用文献

Gong, W.,Hao, B.,Mansy, S.S.,Gonzalez, G.,Gilles-Gonzalez, M.A.,Chan, M.K.
Structure of a biological oxygen sensor: a new mechanism for heme-driven signal transduction.
Proc.Natl.Acad.Sci.USA, 95:15177-15182, 1998

PubMed Abstract: The FixL proteins are biological oxygen sensors that restrict the expression of specific genes to hypoxic conditions. FixL's oxygen-detecting domain is a heme binding region that controls the activity of an attached histidine kinase. The FixL switch is regulated by binding of oxygen and other strong-field ligands. In the absence of bound ligand, the heme domain permits kinase activity. In the presence of bound ligand, this domain turns off kinase activity. Comparison of the structures of two forms of the Bradyrhizobium japonicum FixL heme domain, one in the "on" state without bound ligand and one in the "off" state with bound cyanide, reveals a mechanism of regulation by a heme that is distinct from the classical hemoglobin models. The close structural resemblance of the FixL heme domain to the photoactive yellow protein confirms the existence of a PAS structural motif but reveals the presence of an alternative regulatory gateway.

PubMed: 9860942
DOI: 10.1073/pnas.95.26.15177

実験手法

X-RAY DIFFRACTION (2.4 Å)