1DP6

OXYGEN-BINDING COMPLEX OF FIXL HEME DOMAIN

1DP6 の概要

• エントリーDOI: 10.2210/pdb1dp6/pdb
• 関連するPDBエントリー: 1BV6
• 分子名称: FIXL PROTEIN, OXYGEN MOLECULE, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total)
• 機能のキーワード: fixl, heme, pas domain, signal transduction, histidine kinase, oxygen storage-transport complex, oxygen storage/transport
• 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: 15568.34

構造登録者

Gong, W.,Hao, B.,Chan, M.K. (登録日: 1999-12-23, 公開日: 2000-12-23, 最終更新日: 2024-02-07)

主引用文献

Gong, W.,Hao, B.,Chan, M.K.
New mechanistic insights from structural studies of the oxygen-sensing domain of Bradyrhizobium japonicum FixL.
Biochemistry, 39:3955-3962, 2000

PubMed Abstract: The FixL heme domain serves as the dioxygen switch in the FixL/FixJ two-component system of Rhizobia. Recent structural studies of the Bradyrhizobium japonicum FixL heme domain (BjFixLH) have suggested an allosteric mechanism that is distinct from the classical hemoglobin model. To gain further insight into the FixL sensing mechanism, structures of BjFixLH bound to dioxygen, imidazole, and nitric oxide have been determined. These structures, particularly the structure of BjFixLH bound to its physiological ligand, dioxygen, have helped to address a number of important issues relevant to the BjFixLH sensing mechanism. On the basis of the oxy-BjFixLH structure, a conserved arginine is found to stabilize the dioxygen ligand in a mode reminiscent of the distal histidine in classical myoglobins and hemoglobins. The structure of BjFixLH bound to imidazole elucidates the structural requirements for accommodating sterically bulky ligands. Finally, the structure of BjFixLH bound to nitric oxide provides evidence for a structural intermediate in the heme-driven conformational change.

PubMed: 10747783
DOI: 10.1021/bi992346w

実験手法

X-RAY DIFFRACTION (2.3 Å)