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2KIL

NMR structure of the H103G mutant SO2144 H-NOX domain from Shewanella oneidensis in the Fe(II)CO ligation state

Summary for 2KIL
Entry DOI10.2210/pdb2kil/pdb
Related2kii
NMR InformationBMRB: 16278
DescriptorPutative uncharacterized protein, PROTOPORPHYRIN IX CONTAINING FE, CARBON MONOXIDE, ... (4 entities in total)
Functional Keywordsh-nox, unknown function
Biological sourceShewanella oneidensis
Total number of polymer chains1
Total formula weight21167.08
Authors
Erbil, W.K. (deposition date: 2009-05-06, release date: 2009-11-17, Last modification date: 2024-05-22)
Primary citationErbil, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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