Journal article Open Access

Structure and Function of Sulfotransferases

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


MARC21 XML Export

<?xml version='1.0' encoding='UTF-8'?>
<record xmlns="http://www.loc.gov/MARC21/slim">
  <leader>00000nam##2200000uu#4500</leader>
  <datafield tag="540" ind1=" " ind2=" ">
    <subfield code="u">https://creativecommons.org/publicdomain/zero/1.0/legalcode</subfield>
    <subfield code="a">Creative Commons Zero v1.0 Universal</subfield>
  </datafield>
  <datafield tag="260" ind1=" " ind2=" ">
    <subfield code="c">2001-06-01</subfield>
  </datafield>
  <controlfield tag="005">20200120173032.0</controlfield>
  <controlfield tag="001">1229406</controlfield>
  <datafield tag="909" ind1="C" ind2="O">
    <subfield code="p">openaire</subfield>
    <subfield code="o">oai:zenodo.org:1229406</subfield>
  </datafield>
  <datafield tag="520" ind1=" " ind2=" ">
    <subfield code="a">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 (VO3−4)-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.</subfield>
  </datafield>
  <datafield tag="700" ind1=" " ind2=" ">
    <subfield code="a">Pedersen, Lee G.</subfield>
  </datafield>
  <datafield tag="700" ind1=" " ind2=" ">
    <subfield code="a">Petrotchenko, Evgeniy</subfield>
  </datafield>
  <datafield tag="700" ind1=" " ind2=" ">
    <subfield code="a">Shevtsov, Sergei</subfield>
  </datafield>
  <datafield tag="700" ind1=" " ind2=" ">
    <subfield code="a">Gorokhov, Anna</subfield>
  </datafield>
  <datafield tag="700" ind1=" " ind2=" ">
    <subfield code="a">Kakuta, Yoshimitsu</subfield>
  </datafield>
  <datafield tag="700" ind1=" " ind2=" ">
    <subfield code="a">Pedersen, Lars C.</subfield>
  </datafield>
  <datafield tag="856" ind1="4" ind2=" ">
    <subfield code="s">365604</subfield>
    <subfield code="z">md5:5b5b9e1953fe83a96d388581c260b900</subfield>
    <subfield code="u">https://zenodo.org/record/1229406/files/article.pdf</subfield>
  </datafield>
  <datafield tag="542" ind1=" " ind2=" ">
    <subfield code="l">open</subfield>
  </datafield>
  <datafield tag="980" ind1=" " ind2=" ">
    <subfield code="a">publication</subfield>
    <subfield code="b">article</subfield>
  </datafield>
  <datafield tag="100" ind1=" " ind2=" ">
    <subfield code="a">Negishi, Masahiko</subfield>
  </datafield>
  <datafield tag="024" ind1=" " ind2=" ">
    <subfield code="a">10.1006/abbi.2001.2368</subfield>
    <subfield code="2">doi</subfield>
  </datafield>
  <datafield tag="245" ind1=" " ind2=" ">
    <subfield code="a">Structure and Function of Sulfotransferases</subfield>
  </datafield>
  <datafield tag="650" ind1="1" ind2="7">
    <subfield code="a">cc-by</subfield>
    <subfield code="2">opendefinition.org</subfield>
  </datafield>
</record>
169
281
views
downloads
Views 169
Downloads 281
Data volume 102.7 MB
Unique views 166
Unique downloads 259

Share

Cite as