Analysis of Ca2+/Mg2+ selectivity in α‐lactalbumin and Ca2+‐binding lysozyme reveals a distinct Mg2+‐specific site in lysozyme

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Abstract

The triggering of Ca(2+) signaling pathways relies on Ca(2+)/Mg(2+) specificity of proteins mediating these pathways. Two homologous milk Ca(2+)-binding proteins, bovine alpha-lactalbumin (bLA) and equine lysozyme (EQL), were analyzed using the simplest "four-state" scheme of metal- and temperature-induced structural changes in a protein. The association of Ca(2+)/Mg(2+) by native proteins is entropy-driven. Both proteins exhibit strong temperature dependences of apparent affinities to Ca(2+) and Mg(2+), due to low thermal stabilities of their apo-forms and relatively high unfavorable enthalpies of Mg(2+) association. The ratios of their apparent affinities to Ca(2+) and Mg(2+), being unusually high at low temperatures (5.3-6.5 orders of magnitude), reach the values inherent to classical EF-hand motifs at physiological temperatures. The comparison of phase diagrams predicted within the model of competitive Ca(2+) and Mg(2+) binding with experimental data strongly suggests that the association of Ca(2+) and Mg(2+) ions with bLA is a competitive process, whereas the primary Mg(2+) site of EQL is different from its Ca(2+)-binding site. The later conclusion is corroborated by qualitatively different molar ellipticity changes in near-UV region accompanying Mg(2+) and Ca(2+) association. The Ca(2+)/Mg(2+) selectivity of Mg(2+)-site of EQL is below an order of magnitude. EQL exhibits a distinct Mg(2+)-specific site, probably arising as an adaptation to the extracellular environment.

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