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

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 underst...

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Main Author: Toru Shimizu
Format: Article
Language:English
Published: MDPI AG 2013-06-01
Series:Biosensors
Subjects:
Online Access:http://www.mdpi.com/2079-6374/3/2/211
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author Toru Shimizu
author_facet Toru Shimizu
author_sort Toru Shimizu
collection DOAJ
description 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.
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spelling doaj.art-3e13991000d7464bbc22122544cdc6392022-12-22T02:52:16ZengMDPI AGBiosensors2079-63742013-06-013221123710.3390/bios3020211The Heme-Based Oxygen-Sensor Phosphodiesterase Ec DOS (DosP): Structure-Function RelationshipsToru ShimizuEscherichia 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.http://www.mdpi.com/2079-6374/3/2/211heme proteinoxygen sensorphosphodiesterasec-AMPc-di-GMPsignal transduction
spellingShingle Toru Shimizu
The Heme-Based Oxygen-Sensor Phosphodiesterase Ec DOS (DosP): Structure-Function Relationships
Biosensors
heme protein
oxygen sensor
phosphodiesterase
c-AMP
c-di-GMP
signal transduction
title The Heme-Based Oxygen-Sensor Phosphodiesterase Ec DOS (DosP): Structure-Function Relationships
title_full The Heme-Based Oxygen-Sensor Phosphodiesterase Ec DOS (DosP): Structure-Function Relationships
title_fullStr The Heme-Based Oxygen-Sensor Phosphodiesterase Ec DOS (DosP): Structure-Function Relationships
title_full_unstemmed The Heme-Based Oxygen-Sensor Phosphodiesterase Ec DOS (DosP): Structure-Function Relationships
title_short The Heme-Based Oxygen-Sensor Phosphodiesterase Ec DOS (DosP): Structure-Function Relationships
title_sort heme based oxygen sensor phosphodiesterase ec dos dosp structure function relationships
topic heme protein
oxygen sensor
phosphodiesterase
c-AMP
c-di-GMP
signal transduction
url http://www.mdpi.com/2079-6374/3/2/211
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