Finally! The structural secrets of a HD- GYP phosphodiesterase revealed.

The major sessility-motility lifestyle change and additional fundamental aspects of bacterial physiology, behaviour and morphology are regulated by the secondary messenger cyclic di- GMP (c-di- GMP). Although the c-di- GMP metabolizing enzymes and many receptors have been readily characterized upon discovery, the HD- GYP domain c-di- GMP phosphodiesterase family remained underinvestigated. In this issue of Molecular Microbiology, Bellini et al. provide an important step towards functional and structural characterization of the previously neglected HD- GYP domain family by resolving the crystal structure of PmGH, a catalytically active family member from the thermophilic bacterium Persephonella marina. The crystal structure revealed a novel tri-nuclear catalytic iron centre involved in c-di- GMP binding and catalysis and provides the structural basis to subsequently characterize in detail the catalytic mechanism of hydrolysis of c-di- GMP to GMP by HD- GYP domains. [ABSTRACT FROM AUTHOR]

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