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Biosensors 2013, 3(2), 211-237; doi:10.3390/bios3020211
Review

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

1,2,3,4
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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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.
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
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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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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