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Bacterial physiology

HD-GYP domain structure solved

Nature Reviews Microbiology volume 12, page 4 (2014)Cite this article

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The second messenger cyclic di-GMP, which is involved in many different aspects of bacterial physiology and development, is synthesized by GGDEF-domain diguanylate cyclases (DGCs) and degraded by EAL- or HD-GYP-domain phosphodiesterases (PDEs). Although the DGCs and EAL PDEs have been intensively investigated, much less is known about the HD-GYP PDEs. Bellini et al. now describe the crystal structures of a catalytically active HD-GYP domain protein alone and in complex with its cyclic di-GMP substrate and the final reaction product, GMP. The structures show that the mode of substrate binding differs from that of the EAL PDEs and involves a novel trinuclear, rather than a binuclear, catalytic iron centre.

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References

  1. Bellini, D. et al. Crystal structure of an HD-GYP domain cyclic-di-GMP phosphodiesterase reveals an enzyme with a novel trinuclear catalytic iron centre. Mol. Microbiol. http://dx.doi.org/10.1111/mmi.12447 (2013)

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  1. Sheilagh Molloy
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Molloy, S. HD-GYP domain structure solved. Nat Rev Microbiol 12, 4 (2014). https://doi.org/10.1038/nrmicro3191

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  • DOI: https://doi.org/10.1038/nrmicro3191

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