2KII

NMR structure of the SO2144 H-NOX domain from Shewanella oneidensis in the Fe(II)CO ligation state

2KII の概要

• エントリーDOI: 10.2210/pdb2kii/pdb
• NMR情報: BMRB: 16276
• 分子名称: Putative uncharacterized protein, PROTOPORPHYRIN IX CONTAINING FE, CARBON MONOXIDE (3 entities in total)
• 機能のキーワード: h-nox, unknown function
• 由来する生物種: Shewanella oneidensis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21179.09

構造登録者

Erbil, W.K. (登録日: 2009-05-05, 公開日: 2009-11-17, 最終更新日: 2024-05-22)

主引用文献

Erbil, W.K.,Price, M.S.,Wemmer, D.E.,Marletta, M.A.
A structural basis for H-NOX signaling in Shewanella oneidensis by trapping a histidine kinase inhibitory conformation.
Proc.Natl.Acad.Sci.USA, 106:19753-19760, 2009

PubMed Abstract: Heme nitric oxide/oxygen (H-NOX) proteins are found in eukaryotes where they are typically part of a larger protein such as soluble guanylate cyclase and in prokaryotes where they are often found in operons with a histidine kinase, suggesting that H-NOX proteins serve as sensors for NO and O(2) in signaling pathways. The Fe(II)-NO complex of the H-NOX protein from Shewanella oneidensis inhibits the autophosphorylation of the operon-associated histidine kinase, whereas the ligand-free H-NOX has no effect on the kinase. NMR spectroscopy was used to determine the structures of the Fe(II)-CO complex of the S. oneidensis H-NOX and the Fe(II)-CO complex of the H103G H-NOX mutant as a mimic of the ligand-free and kinase-inhibitory Fe(II)-NO H-NOX, respectively. The results provide a molecular glimpse into the ligand-induced conformational changes that may underlie kinase inhibition and the subsequent control of downstream signaling.

PubMed: 19918063
DOI: 10.1073/pnas.0911645106

実験手法

SOLUTION NMR