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Structural basis for calcium binding by uteroglobins

H J Barnes1, L Nordlund-Möller, M Nord

  • 1Center for Structural Biochemistry, NOVUM, S-141 57, Huddinge, Sweden.

Journal of Molecular Biology
|February 23, 1996
PubMed
Summary
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Researchers identified a calcium-binding site in human uteroglobin, structurally similar to phospholipase A2 enzymes. Mutating Asp46 significantly reduced calcium binding, confirming its crucial role in uteroglobin

Area of Science:

  • Structural Biology
  • Biochemistry
  • Computational Biology

Background:

  • Uteroglobins are proteins found in various species, including humans, with structural and ligand-binding similarities to rabbit uteroglobin.
  • Human uteroglobin has been shown to bind calcium, prompting an investigation into its metal-binding capabilities.
  • Uteroglobin's three-dimensional structure and potential metal-binding sites are not fully elucidated.

Purpose of the Study:

  • To computationally identify potential metal-binding sites within the three-dimensional structure of uteroglobin.
  • To investigate the role of specific residues, particularly Asp46, in calcium binding.
  • To compare the identified calcium-binding site with known metal-binding sites in other proteins.

Main Methods:

  • Utilized two computational procedures, including hydrophobic contrast function analysis, to predict metal-binding sites.

Related Experiment Videos

  • Employed molecular dynamics with a restrained calcium ion for conformational optimization and valence calculations.
  • Performed site-directed point mutagenesis (Asp46 to Asn or Lys) and assessed calcium binding using ruthenium red and 45Ca2+.

    • Main Results:

    • A putative calcium-binding site in uteroglobin was identified, structurally resembling the primary calcium-binding site of secretory phospholipase A2 enzymes.
    • This motif, involving an aspartic acid residue and backbone carbonyl oxygens, is conserved across different species' uteroglobins.
    • Mutagenesis of Asp46 significantly reduced ruthenium red and 45Ca2+ binding, indicating its critical role. Mutant proteins retained dimerization ability.

    Conclusions:

    • Asp46 in uteroglobins functions as a 'cap' residue within a calcium-binding site.
    • The identified calcium-binding site shares structural similarities with those found in phospholipase A2 enzymes.
    • These findings provide insights into the structural basis of calcium binding in uteroglobins and their potential functional implications.