Structure and function of sulfotransferases

Masahiko Negishi, Lee G. Pedersen, Evgeniy Petrotchenko, Sergei Shevtsov, Anna Gorokhov, Yoshimitsu Kakuta, Lars C. Pedersen

Research output: Contribution to journalArticlepeer-review

238 Citations (Scopus)

Abstract

Sulfotransferases (STs) catalyze the transfer reaction of the sulfate group from the ubiquitous donor 3′-phosphoadenosine 5′-phosphosulfate (PAPS) to an acceptor group of numerous substrates. This reaction, often referred to as sulfuryl transfer, sulfation, or sulfonation, is widely observed from bacteria to humans and plays a key role in various biological processes such as cell communication, growth and development, and defense. The cytosolic STs sulfate small molecules such as steroids, bioamines, and therapeutic drugs, while the Golgi-membrane counterparts sulfate large molecules including glucosaminylglycans and proteins. We have now solved the X-ray crystal structures of four cytosolic and one membrane ST. All five STs are globular proteins composed of a single α/β domain with the characteristic five-stranded β-sheet. The β-sheet constitutes the core of the Paps-binding and catalytic sites. Structural analysis of the PAPS-, PAP-, substrate-, and/or orthovanadate (VO4 3-)-bound enzymes has also revealed the common molecular mechanism of the transfer reaction catalyzed by sulfotransferses. The X-ray crystal structures have opened a new era for the study of sulfotransferases.

Original languageEnglish
Pages (from-to)149-157
Number of pages9
JournalArchives of Biochemistry and Biophysics
Volume390
Issue number2
DOIs
Publication statusPublished - Jun 15 2001
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology

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