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Related Experiment Videos

Structure and function of radical SAM enzymes.

Gunhild Layer1, Dirk W Heinz, Dieter Jahn

  • 1Divison of Structural Biology, German Research Center for Biotechnology (GBF), Mascheroder Weg 1, D-38124 Braunschweig, Germany.

Current Opinion in Chemical Biology
|September 29, 2004
PubMed
Summary

Radical SAM enzymes use a [4Fe-4S] cluster and S-adenosyl-l-methionine (SAM) to create radicals. Crystal structures reveal unique cofactor coordination, highlighting protein scaffold plasticity for diverse enzyme functions.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Radical SAM enzymes are a large enzyme family characterized by a [4Fe-4S] cluster and S-adenosyl-l-methionine (SAM).
  • These enzymes generate highly reactive 5'-deoxyadenosyl radicals essential for various biochemical transformations.
  • Understanding their structure-function relationship is crucial due to their diverse roles in metabolism and disease.

Purpose of the Study:

  • To elucidate the structural basis of cofactor positioning and coordination in Radical SAM enzymes.
  • To compare the structural features of oxygen-independent coproporphyrinogen III oxidase (HemN) and biotin synthase.
  • To identify conserved and variable elements within the Radical SAM enzyme family.

Main Methods:

  • X-ray crystallography to determine the 3D structures of HemN and biotin synthase.

Related Experiment Videos

  • Biochemical and biophysical techniques to support structural findings.
  • Electron Nuclear Double Resonance (ENDOR) spectroscopy to confirm cofactor interactions.

    • Main Results:

    • Detailed crystal structures of HemN and biotin synthase revealed the precise arrangement of the [4Fe-4S] cluster and SAM.
    • A novel coordination environment was observed, with direct ligation of the [4Fe-4S] cluster by SAM's methionine moiety.
    • Structural data revealed conserved features across the family, alongside plasticity in the protein scaffold.

    Conclusions:

    • The study provides unprecedented structural insights into Radical SAM enzyme mechanisms.
    • Conserved structural elements facilitate cofactor binding and radical generation across the family.
    • The observed plasticity of the protein scaffold explains the functional accommodation of over 600 Radical SAM enzymes.