Abstract
The intracellular level of the ubiquitous bacterial secondary messenger, cyclic di-(3′,5′)-guanosine monophosphate (c-di-GMP), represents a balance between its biosynthesis and degradation, the latter via specific phosphodiesterases (PDEs). One class of c-di-GMP PDEs contains a characteristic HD-GYP domain. Here we report that an HD-GYP PDE from Vibrio cholerae contains a non-heme diiron-carboxylate active site, and that only the reduced form is active. An engineered D-to-A substitution in the HD dyad caused loss of c-di-GMP PDE activity and of two iron atoms. This report constitutes the first demonstration that a non-heme diiron-carboxylate active site can catalyze the c-di-GMP PDE reaction and that this activity can be redox regulated in the HD-GYP class.
Original language | English (US) |
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Pages (from-to) | 5329-5331 |
Number of pages | 3 |
Journal | Biochemistry |
Volume | 52 |
Issue number | 32 |
DOIs | |
State | Published - Aug 13 2013 |
ASJC Scopus subject areas
- Biochemistry