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Histidine phosphorylation in metalloprotein binding sites.

Cheryl L Mathis1, Amy M Barrios1

  • 1Department of Medicinal Chemistry, College of Pharmacy, University of Utah, Salt Lake City, UT 84112, United States.

Journal of Inorganic Biochemistry
|September 23, 2021
PubMed
Summary

Histidine phosphorylation, a largely unexplored post-translational modification, impacts metalloprotein function by altering metal coordination. This review explores its regulatory role in eleven metalloproteins.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Post-translational modifications (PTMs) regulate protein function, but histidine phosphorylation remains understudied compared to serine, threonine, and tyrosine.
  • Phosphorylated histidine's instability poses challenges, yet its unique metal-binding properties warrant investigation.
  • Histidine's role in metal coordination suggests phosphorylation could significantly alter metalloprotein characteristics.

Purpose of the Study:

  • To review the current understanding of histidine phosphorylation in metalloproteins.
  • To explore how phosphohistidine affects metal binding and protein structure/conformation.
  • To discuss methods and challenges in studying histidine phosphorylation in metalloproteins.

Main Methods:

  • Literature review of eleven metalloproteins exhibiting reversible histidine phosphorylation.
  • Analysis of protein structure and biological activity.
  • Emphasis on the impact of phosphohistidine on metal coordination spheres and protein conformation.

Main Results:

  • Eleven metalloproteins were identified with histidine phosphorylation near metal-binding sites.
  • Phosphohistidine can modulate the primary coordination sphere and influence protein conformation.
  • The study highlights the potential regulatory role of histidine phosphorylation in metalloprotein function.

Conclusions:

  • Histidine phosphorylation is a significant, yet underexplored, regulatory mechanism in metalloproteins.
  • Understanding phosphohistidine's impact on metal coordination is crucial for deciphering metalloprotein regulation.
  • Further research is needed to overcome challenges in studying this PTM and its functional consequences.