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Mammalian metallothionein.

J H Kägi1, P Hunziker

  • 1Biochemisches Institut der Universität Zürich, Switzerland.

Biological Trace Element Research
|July 1, 1989
PubMed
Summary
This summary is machine-generated.

Metallothioneins (MTs) are bioinorganic proteins rich in metals and cysteine. Structural studies confirm a two-cluster model for metal binding in mammalian MTs, revealing conserved sequences and genetic polymorphism.

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Area of Science:

  • Bioinorganic Chemistry
  • Structural Biology
  • Biochemistry

Background:

  • Metallothioneins (MTs) are polypeptidic bioinorganic structures characterized by high metal and cysteine content, forming metal-thiolate clusters.
  • MTs are classified into three groups based on structural criteria, with Class I including mammalian MTs.
  • Over 50 amino acid sequences are known, revealing significant conservation (over 55% residues, including 20 Cys) in mammalian MTs.

Purpose of the Study:

  • To investigate the structural basis of metal binding in metallothioneins.
  • To confirm the proposed two-cluster model for metal-thiolate cluster formation in mammalian MTs.
  • To elucidate the spatial structures of specific mammalian MTs.

Main Methods:

  • Chemical, spectroscopic, and structural analyses of metallothioneins.

Related Experiment Videos

  • Amino acid and nucleotide sequencing to determine MT structures and identify polymorphism.
  • 2D Nuclear Magnetic Resonance (NMR) spectroscopy in aqueous solution to determine the spatial structures of rat MT-2 and rabbit MT-2a.

    • Main Results:

    • The study confirms the classification of MTs into three classes.
    • Mammalian MTs exhibit genetic polymorphism, with multiple functional isoMTs identified in humans and rabbits.
    • The spatial structures of rat MT-2 and rabbit MT-2a confirm the two-cluster model for binding seven bivalent metal ions (Me(II)3(Cys)9 and Me(II)4(Cys)11) via thiolate coordination.

    Conclusions:

    • The two-cluster model for metal-thiolate cluster formation in mammalian metallothioneins is structurally validated.
    • Metallothioneins play a significant role in metal homeostasis and detoxification, with conserved structural features across species.
    • Genetic polymorphism in MTs contributes to functional diversity and adaptation.