Structural domain plasticity drives Zn(II) distribution and buffering in metallothionein-3
Manuel David Peris-Díaz1,2, Eduard H T M Ebberink1, Jan Fiala1
1Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht 3584 CH, The Netherlands.
Abstract:
Complementary mass spectrometry-based approaches and molecular dynamics simulations were integrated to map Zn(II) distribution in partially metalated Zn4-6-metallothionein-3 species relevant to zinc metabolism. Sequential Zn(II) dissociation engages both the α- and β-domains through a structurally plastic, interdomain mechanism that underpins regulatory zinc buffering at physiological pZn.
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