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Biosensors 2013, 3(2), 211-237;

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

Department of Cell Biology, Shantou University Medical College, Shantou 515041, China
Department of Biochemistry, Charles University in Prague, Prague 2, 128 43, Czech Republic
Department of Medical Biotechnology, Jagiollonian University, Krakow 30-387, Poland
Research Center for Compact Chemical System, National Institute of Advanced Industrial Science and Technology (AIST), Sendai 983-8551, Japan
Received: 24 April 2013 / Revised: 24 May 2013 / Accepted: 13 June 2013 / Published: 17 June 2013
(This article belongs to the Special Issue Physiological Sensors of Gases, Light, Redox State and Hypoxia)
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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. View Full-Text
Keywords: heme protein; oxygen sensor; phosphodiesterase; c-AMP; c-di-GMP; signal transduction heme protein; oxygen sensor; phosphodiesterase; c-AMP; c-di-GMP; signal transduction

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Shimizu, T. The Heme-Based Oxygen-Sensor Phosphodiesterase Ec DOS (DosP): Structure-Function Relationships. Biosensors 2013, 3, 211-237.

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