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Related Experiment Videos

Structure and function of sulfotransferases.

M Negishi1, L G Pedersen, E Petrotchenko

  • 1Pharmacogenetics Section, Laboratory of Reproductive and Developmental Toxicology, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, North Carolina 27709, USA. negishi@niehs.nih.gov

Archives of Biochemistry and Biophysics
|June 9, 2001
PubMed
Summary
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Sulfotransferases (STs) are crucial enzymes involved in biological processes. Their X-ray crystal structures reveal common mechanisms for sulfate transfer, advancing the study of these vital proteins.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Sulfotransferases (STs) catalyze the transfer of sulfate groups from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to various substrates.
  • This sulfation reaction is essential for diverse biological functions, including cell communication, development, and defense, across organisms from bacteria to humans.
  • STs are categorized into cytosolic and Golgi-membrane bound enzymes, differing in their substrate specificity and localization.

Purpose of the Study:

  • To elucidate the structural basis of sulfotransferase function.
  • To understand the molecular mechanism of the sulfation reaction catalyzed by STs.
  • To provide high-resolution structural insights into both cytosolic and membrane-bound sulfotransferases.

Main Methods:

Related Experiment Videos

  • X-ray crystallography was employed to determine the three-dimensional structures of five sulfotransferases (four cytosolic, one membrane-bound).
  • Structural analysis included enzymes bound to PAPS, PAP, substrates, and orthovanadate (VO(3-)(4)).
  • Comparative structural analysis was performed to identify common features and mechanisms.

    • Main Results:

    • The X-ray crystal structures of four cytosolic and one membrane ST were solved, revealing globular proteins with a conserved alpha/beta domain and a five-stranded beta-sheet.
    • The beta-sheet forms the core of the PAPS-binding and catalytic sites in all studied STs.
    • Structural data elucidated a common molecular mechanism underlying the transfer reaction catalyzed by sulfotransferases.

    Conclusions:

    • The determined X-ray crystal structures provide unprecedented atomic-level detail of sulfotransferases.
    • These structures reveal conserved structural elements and a common catalytic mechanism for the sulfation reaction.
    • The structural insights mark a significant advancement in the field, opening new avenues for sulfotransferase research.