An HD-GYP cyclic di-guanosine monophosphate phosphodiesterase with a non-heme diiron-carboxylate active site

Kyle D. Miner, Karl E. Klose, Donald M. Kurtz

Research output: Contribution to journalArticle

13 Scopus citations

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 languageEnglish (US)
Pages (from-to)5329-5331
Number of pages3
JournalBiochemistry
Volume52
Issue number32
DOIs
StatePublished - Aug 13 2013
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry

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