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Zinc Chemistry in Function and Structure of Zinc Proteins

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Methods in Protein Sequence Analysis

Part of the book series: Advances in Life Sciences ((ALS))

Summary

The flexible coordination sphere of zinc, its amphoteric nature and its stable d shell are all properties that are critical to its biological utilization and versatility. The crystal structures of 12 zinc enzymes identify common features of their zinc binding sites. Catalytic zinc is bound by 3 protein ligands with a frequency of His ≫ Glu > Asp = Cys. “Short” spacers (1–3 amino acids) separate the first 2 ligands. “Long” spacers (19–123 amino acids) separate them from the third ligand. Activated water completes the coordination sphere. Structural zinc sites are coordinated by 4 cysteines. A zinc cluster structure, discovered in metallothionein, is now observed in the transcription factor GAL4.

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Authors and Affiliations

  1. Harvard Medical School, Center for Biochemical and Biophysical Sciences and Medicine, 250 Longwood Ave, Boston, MA, 02115, USA

    Bert L. Vallee & David S. Auld

Authors
  1. Bert L. Vallee
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  2. David S. Auld
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Editors and Affiliations

  1. Department of Chemistry I, Karolinska Institute, S-104 01, Stockholm, Sweden

    Hans Jörnvall , Jan-Olov Höög  & Ann-Margreth Gustavsson ,  & 

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© 1991 Springer Basel AG

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Vallee, B.L., Auld, D.S. (1991). Zinc Chemistry in Function and Structure of Zinc Proteins. In: Jörnvall, H., Höög, JO., Gustavsson, AM. (eds) Methods in Protein Sequence Analysis. Advances in Life Sciences. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-5678-2_37

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  • DOI: https://doi.org/10.1007/978-3-0348-5678-2_37

  • Publisher Name: Birkhäuser, Basel

  • Print ISBN: 978-3-0348-5680-5

  • Online ISBN: 978-3-0348-5678-2

  • eBook Packages: Springer Book Archive

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