An HD-GYP Cyclic Di-Guanosine Monophosphate Phosphodiesterase with a Non-Heme Diiron-Carboxylate Active Site

作者：Miner Kyle D; Klose Karl E; Kurtz Donald M Jr^*

来源：Biochemistry, 2013, 52(32): 5329-5331.

DOI：10.1021/bi4009215

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.

• 出版日期2013-8-13