Heme Ligand Binding Properties and Intradimer Interactions in the Full-length Sensor Protein Dos from Escherichia coli and Its Isolated Heme Domain

Dos from Escherichia coli is a bacterial gas sensor protein comprising a heme-containing gas sensor domain and a phosphodiesterase catalytic domain. Using a combination of static light scattering and gel filtration experiments, we established that, as are many other sensor proteins, the full-length...

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Bibliographic Details
Published in:The Journal of biological chemistry 2009-12, Vol.284 (52), p.36146-36159
Main Authors: Lechauve, Christophe, Bouzhir-Sima, Latifa, Yamashita, Taku, Marden, Michael C., Vos, Marten H., Liebl, Ursula, Kiger, Laurent
Format: Article
Language:English
Subjects:
Carbon Monoxide - chemistry
Carbon Monoxide - metabolism
Escherichia coli
Escherichia coli - enzymology
Escherichia coli Proteins - chemistry
Escherichia coli Proteins - metabolism
Heme - chemistry
Heme - metabolism
Ligands
Mechanisms of Signal Transduction
Oxygen - chemistry
Oxygen - metabolism
Phosphoric Diester Hydrolases - chemistry
Phosphoric Diester Hydrolases - metabolism
Protein Multimerization - physiology
Protein Structure, Quaternary - physiology
Protein Structure, Tertiary - physiology
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Summary:Dos from Escherichia coli is a bacterial gas sensor protein comprising a heme-containing gas sensor domain and a phosphodiesterase catalytic domain. Using a combination of static light scattering and gel filtration experiments, we established that, as are many other sensor proteins, the full-length protein is dimeric. The full-length dimer (association constant
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M109.066811