Crystal structure of SULT2A3, human hydroxysteroid sulfotransferase.

Article Details

Citation

Pedersen LC, Petrotchenko EV, Negishi M

Crystal structure of SULT2A3, human hydroxysteroid sulfotransferase.

FEBS Lett. 2000 Jun 9;475(1):61-4.

PubMed ID
10854859 [ View in PubMed
]
Abstract

The crystal structure of SULT2A3 human hydroxysteroid sulfotransferase has been solved at 2.4 A resolution in the presence of 3'-phosphoadenosine 5'-phosphate (PAP). The overall structure is similar to those of SULT1 enzymes such as estrogen sulfotransferase and the PAP binding site is conserved, however, significant differences exist in the positions of loops Pro14-Ser20, Glu79-Ile82 and Tyr234-Gln244 in the substrate binding pocket. Moreover, protein interaction in the crystal structure has revealed a possible dimer-directed conformational alteration that may regulate the SULT activity.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Sulfotransferase 2A1Q06520Details