A structural basis for H-NOX signaling in Shewanella oneidensis by trapping a histidine kinase inhibitory conformation

W. Kaya Erbil, Mark S. Price, David E. Wemmer, Michael A. Marletta

Research output: Contribution to journalArticlepeer-review

63 Scopus citations

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 O2 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 down-stream signaling.

Original languageEnglish (US)
Pages (from-to)19753-19760
Number of pages8
JournalProceedings of the National Academy of Sciences of the United States of America
Volume106
Issue number47
DOIs
StatePublished - Nov 24 2009

Keywords

  • Hemoprotein
  • NMR
  • Nitric oxide
  • Phosphorylation
  • Signaling

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