%0 Journal Article
%T The Heme-Based Oxygen-Sensor Phosphodiesterase Ec DOS (DosP): Structure-Function Relationships
%A Toru Shimizu
%J Biosensors
%D 2013
%I MDPI AG
%R 10.3390/bios3020211
%X Escherichia coli Direct Oxygen Sensor ( Ec DOS, also known as Ec DosP) is a heme-based O 2-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 O 2-sensing PAS domain and a C-terminal phosphodiesterase catalytic domain. Notably, its activity is markedly enhanced by O 2 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 O 2 binding. This review summarizes the intriguing findings that have obtained for Ec DOS.
%K heme protein
%K oxygen sensor
%K phosphodiesterase
%K c-AMP
%K c-di-GMP
%K signal transduction
%U http://www.mdpi.com/2079-6374/3/2/211