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 journalArticle

225 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

Fingerprint

Sulfotransferases
Phosphoadenosine Phosphosulfate
Sulfates
Crystal structure
X-Rays
Membranes
Biological Phenomena
X rays
Sulfonation
Molecules
Vanadates
Substrates
Growth and Development
Structural analysis
Cell Communication
Catalytic Domain
Bacteria
Proteins
Steroids
Binding Sites

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology

Cite this

Negishi, M., Pedersen, L. G., Petrotchenko, E., Shevtsov, S., Gorokhov, A., Kakuta, Y., & Pedersen, L. C. (2001). Structure and function of sulfotransferases. Archives of Biochemistry and Biophysics, 390(2), 149-157. https://doi.org/10.1006/abbi.2001.2368

Structure and function of sulfotransferases. / Negishi, Masahiko; Pedersen, Lee G.; Petrotchenko, Evgeniy; Shevtsov, Sergei; Gorokhov, Anna; Kakuta, Yoshimitsu; Pedersen, Lars C.

In: Archives of Biochemistry and Biophysics, Vol. 390, No. 2, 15.06.2001, p. 149-157.

Research output: Contribution to journalArticle

Negishi, M, Pedersen, LG, Petrotchenko, E, Shevtsov, S, Gorokhov, A, Kakuta, Y & Pedersen, LC 2001, 'Structure and function of sulfotransferases', Archives of Biochemistry and Biophysics, vol. 390, no. 2, pp. 149-157. https://doi.org/10.1006/abbi.2001.2368
Negishi M, Pedersen LG, Petrotchenko E, Shevtsov S, Gorokhov A, Kakuta Y et al. Structure and function of sulfotransferases. Archives of Biochemistry and Biophysics. 2001 Jun 15;390(2):149-157. https://doi.org/10.1006/abbi.2001.2368
Negishi, Masahiko ; Pedersen, Lee G. ; Petrotchenko, Evgeniy ; Shevtsov, Sergei ; Gorokhov, Anna ; Kakuta, Yoshimitsu ; Pedersen, Lars C. / Structure and function of sulfotransferases. In: Archives of Biochemistry and Biophysics. 2001 ; Vol. 390, No. 2. pp. 149-157.
@article{3d864d1645cf44eb98fa1810a4929be4,
title = "Structure and function of sulfotransferases",
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.",
author = "Masahiko Negishi and Pedersen, {Lee G.} and Evgeniy Petrotchenko and Sergei Shevtsov and Anna Gorokhov and Yoshimitsu Kakuta and Pedersen, {Lars C.}",
year = "2001",
month = "6",
day = "15",
doi = "10.1006/abbi.2001.2368",
language = "English",
volume = "390",
pages = "149--157",
journal = "Archives of Biochemistry and Biophysics",
issn = "0003-9861",
publisher = "Academic Press Inc.",
number = "2",

}

TY - JOUR

T1 - Structure and function of sulfotransferases

AU - Negishi, Masahiko

AU - Pedersen, Lee G.

AU - Petrotchenko, Evgeniy

AU - Shevtsov, Sergei

AU - Gorokhov, Anna

AU - Kakuta, Yoshimitsu

AU - Pedersen, Lars C.

PY - 2001/6/15

Y1 - 2001/6/15

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0035876188&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035876188&partnerID=8YFLogxK

U2 - 10.1006/abbi.2001.2368

DO - 10.1006/abbi.2001.2368

M3 - Article

C2 - 11396917

AN - SCOPUS:0035876188

VL - 390

SP - 149

EP - 157

JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

SN - 0003-9861

IS - 2

ER -