Coronavirus (Covid-19): Latest updates and information
Skip to main content Skip to navigation

Histidines in metallothioneins

Previously characterised metallothioneins from yeast, vertebrates, and other animals coordinate metal ions exclusively through thiolate sulfurs. Up until fairly recently, this was a paradigm of metallothioneins. However, quite a number of metallothioneins do contain histidine residues, which may in principle also coordinate metal ions through their imidazole nitrogens (see: Histidines in metallothioneins (JIB 2008)).

We have currently several metallothioneins under study in our lab in which histidine residues play pivotal roles in modulating the metal-binding properties of these intriguing residues.

  • Bacterial metallothioneins homologous to SmtA contain at least one Cys3His site. The His residue in these appears to be vital for an ordered structure in the C-terminal part of these proteins (see: Role of histidines in bacterial MTs (JBIC 2007))his40_detail.jpg

Picture based on pdb 1jjd (Blindauer et al., PNAS 2001).

ec_domii.jpg

Picture based on pdb 2kak (Peroza et al., J. Mol. Biol. 2009)