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Structure and Function of HD-GYP Phosphodiesterases

  • Serena Rinaldo
  • Alessandro Paiardini
  • Alessio Paone
  • Francesca CutruzzolàEmail author
  • Giorgio Giardina
Chapter
  • 114 Downloads

Abstract

HD-GYPs represent the least abundant, and somewhat mysterious, class of dedicated cyclic di-GMP phosphodiesterases (PDE). They are metal dependent enzymes, belonging to the HD phosphohydrolase superfamily, and are evolutionarily unrelated to the EAL class of cyclic di-GMP dedicated PDEs. In contrast to the EAL domain that hydrolyses cyclic di-GMP to pGpG, HD-GYPs are able to further hydrolyse pGpG to GMP. As both the GGDEF and EAL domains, the HD-GYP module is often found fused with other regulatory domains. Despite the ability to act as a PDE, the physiological role(s) of HD-GYP proteins within the cyclic di-GMP-dependent biofilm regulation are still not fully clarified. Indeed, many HD-GYPs may also mediate protein−protein interactions within more complex regulatory pathways or function as cyclic di-GMP or pGpG receptors. The few structures available indicate that HD-GYPs can be clustered into two distinct groups depending on the metal binding site, which can accommodate two or three metal ions. The nature and the number of bound metals determine whether a certain HD-GYP will be active as a PDE or will function as a dinucleotide binding domain. In this chapter, we will review the biochemical and structural data available to date on HD-GYPs.

Keywords

HD-GYP Phosphodiesterase pGpG Cyclic di-GMP 

Notes

Acknowledgements

The authors would like to acknowledge Sapienza University of Rome (Italy) [to FC RP11715C644A5CCE and SR RM11715C646D693E] for financial support. Dr. Giovanna Boumis is acknowledged for fruitful discussions.

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Copyright information

© Springer Nature Switzerland AG 2020

Authors and Affiliations

  • Serena Rinaldo
    • 1
    • 2
  • Alessandro Paiardini
    • 1
    • 2
  • Alessio Paone
    • 1
    • 2
  • Francesca Cutruzzolà
    • 1
    • 2
    Email author
  • Giorgio Giardina
    • 1
    • 2
  1. 1.Department of Biochemical Sciences “A. Rossi Fanelli”Sapienza University of Rome (I)RomeItaly
  2. 2.Istituto Pasteur Italia-Fondazione Cenci BolognettiRomeItaly

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