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

Biosensors

关键词: heme protein;    oxygen sensor;    phosphodiesterase;    c-AMP;    c-di-GMP;    signal transduction;   

DOI  :  10.3390/bios3020211

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2013 by the authors; licensee MDPI, Basel, Switzerland.