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The Heme-Based Oxygen-Sensor Phosphodiesterase Ec DOS (DosP): Structure-Function Relationships.

Shimizu T - Biosensors (Basel) (2013)

Bottom Line: Notably, its activity is markedly enhanced by O2 binding to the heme Fe(II) complex in the PAS sensor domain.X-ray crystal structures and spectroscopic and catalytic characterization of the wild-type and mutant proteins have provided important structural and functional clues to understanding the molecular mechanism of intramolecular catalytic regulation by O2 binding.This review summarizes the intriguing findings that have obtained for Ec DOS.

View Article: PubMed Central - PubMed

Affiliation: Department of Cell Biology, Shantou University Medical College, Shantou 515041, China. shimizu@tagen.tohoku.ac.jp.

ABSTRACT
Escherichia coli Direct Oxygen Sensor (Ec DOS, also known as Ec DosP) is a heme-based O2-sensing phosphodiesterase from Escherichia coli that catalyzes the conversion of cyclic-di-GMP to linear di-GMP. Cyclic-di-GMP is an important second messenger in bacteria, highlighting the importance of understanding structure-function relationships of Ec DOS. Ec DOS is composed of an N-terminal heme-bound O2-sensing PAS domain and a C-terminal phosphodiesterase catalytic domain. Notably, its activity is markedly enhanced by O2 binding to the heme Fe(II) complex in the PAS sensor domain. X-ray crystal structures and spectroscopic and catalytic characterization of the wild-type and mutant proteins have provided important structural and functional clues to understanding the molecular mechanism of intramolecular catalytic regulation by O2 binding. This review summarizes the intriguing findings that have obtained for Ec DOS.

No MeSH data available.


Related in: MedlinePlus

Both Ec DOS and AxPDEA1 are heme-based oxygen-sensor PDEs toward c-di-GMP. The EAL domain associated with PDE is located in the C-terminal domain. The activity of Ec DOS is enhanced by O2 binding to the heme Fe(II) complex, whereas that of AxPDEA1 is enhanced by O2 dissociation from the heme Fe(II) complex [11,12,20,23,24,25,26].
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biosensors-03-00211-f004: Both Ec DOS and AxPDEA1 are heme-based oxygen-sensor PDEs toward c-di-GMP. The EAL domain associated with PDE is located in the C-terminal domain. The activity of Ec DOS is enhanced by O2 binding to the heme Fe(II) complex, whereas that of AxPDEA1 is enhanced by O2 dissociation from the heme Fe(II) complex [11,12,20,23,24,25,26].

Mentions: On the basis of the amino acid sequence of Ec DOS, it was predicted that the PDE activity of this enzyme toward c-di-GMP is regulated by O2 association with, or dissociation from, the N-terminal PAS domain-bound heme Fe(II) complex [20]. Physicochemical studies have been carried out using the isolated heme-bound PAS domain of Ec DOS (Ec DOS-PAS-A) [21]. The initial studies using c-AMP as a substrate characterized the catalytic activities of Ec DOS because of difficulties in obtaining sufficient quantities of high-quality c-di-GMP (see below) [22]. In contrast, the PDE catalytic activity of AxPEDA1, a heme-based oxygen-sensor PDE from Acetobacter xylinum, toward c-di-GMP has been more directly characterized. These studies have shown that the activity of this enzyme is stimulated by O2 dissociation from the heme Fe(II) complex (Figure 4) [23].


The Heme-Based Oxygen-Sensor Phosphodiesterase Ec DOS (DosP): Structure-Function Relationships.

Shimizu T - Biosensors (Basel) (2013)

Both Ec DOS and AxPDEA1 are heme-based oxygen-sensor PDEs toward c-di-GMP. The EAL domain associated with PDE is located in the C-terminal domain. The activity of Ec DOS is enhanced by O2 binding to the heme Fe(II) complex, whereas that of AxPDEA1 is enhanced by O2 dissociation from the heme Fe(II) complex [11,12,20,23,24,25,26].
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4263535&req=5

biosensors-03-00211-f004: Both Ec DOS and AxPDEA1 are heme-based oxygen-sensor PDEs toward c-di-GMP. The EAL domain associated with PDE is located in the C-terminal domain. The activity of Ec DOS is enhanced by O2 binding to the heme Fe(II) complex, whereas that of AxPDEA1 is enhanced by O2 dissociation from the heme Fe(II) complex [11,12,20,23,24,25,26].
Mentions: On the basis of the amino acid sequence of Ec DOS, it was predicted that the PDE activity of this enzyme toward c-di-GMP is regulated by O2 association with, or dissociation from, the N-terminal PAS domain-bound heme Fe(II) complex [20]. Physicochemical studies have been carried out using the isolated heme-bound PAS domain of Ec DOS (Ec DOS-PAS-A) [21]. The initial studies using c-AMP as a substrate characterized the catalytic activities of Ec DOS because of difficulties in obtaining sufficient quantities of high-quality c-di-GMP (see below) [22]. In contrast, the PDE catalytic activity of AxPEDA1, a heme-based oxygen-sensor PDE from Acetobacter xylinum, toward c-di-GMP has been more directly characterized. These studies have shown that the activity of this enzyme is stimulated by O2 dissociation from the heme Fe(II) complex (Figure 4) [23].

Bottom Line: Notably, its activity is markedly enhanced by O2 binding to the heme Fe(II) complex in the PAS sensor domain.X-ray crystal structures and spectroscopic and catalytic characterization of the wild-type and mutant proteins have provided important structural and functional clues to understanding the molecular mechanism of intramolecular catalytic regulation by O2 binding.This review summarizes the intriguing findings that have obtained for Ec DOS.

View Article: PubMed Central - PubMed

Affiliation: Department of Cell Biology, Shantou University Medical College, Shantou 515041, China. shimizu@tagen.tohoku.ac.jp.

ABSTRACT
Escherichia coli Direct Oxygen Sensor (Ec DOS, also known as Ec DosP) is a heme-based O2-sensing phosphodiesterase from Escherichia coli that catalyzes the conversion of cyclic-di-GMP to linear di-GMP. Cyclic-di-GMP is an important second messenger in bacteria, highlighting the importance of understanding structure-function relationships of Ec DOS. Ec DOS is composed of an N-terminal heme-bound O2-sensing PAS domain and a C-terminal phosphodiesterase catalytic domain. Notably, its activity is markedly enhanced by O2 binding to the heme Fe(II) complex in the PAS sensor domain. X-ray crystal structures and spectroscopic and catalytic characterization of the wild-type and mutant proteins have provided important structural and functional clues to understanding the molecular mechanism of intramolecular catalytic regulation by O2 binding. This review summarizes the intriguing findings that have obtained for Ec DOS.

No MeSH data available.


Related in: MedlinePlus