Crystal Structures of Candida albicans Phosphodiesterase 2 and Implications for Its Biological Functions.

ABSTRACT: The cAMP signaling system plays important roles in the physiological processes of pathogen yeast Candida albicans, but its functional mechanism has not been well illustrated. Here, we report the enzymatic characterization and crystal structures of C. albicans phosphodiesterase 2 (caPDE2) in the unliganded and 3-isobutyl-1-methylxanthine-complexed forms. caPDE2 is a monomer in liquid and crystal states and specifically hydrolyzes cAMP with a K_M of 35 nM. It does not effectively hydrolyze cGMP as shown by the 1.32 × 10⁵-fold specificity of cAMP/cGMP. The crystal structure of caPDE2 shows significant differences from those of human PDEs. First, the N-terminal fragment of caPDE2 (residues 1-201) tightly associates with the catalytic domain to form a rigid molecular entity

SUBMITTER: Yao T 

PROVIDER: S-EPMC9364965 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature