Structural highlights
Function
[ST2A1_HUMAN] Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfonation of steroids and bile acids in the liver and adrenal glands.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Crystal structure of SULT2A3, human hydroxysteroid sulfotransferase.,Pedersen LC, Petrotchenko EV, Negishi M FEBS Lett. 2000 Jun 9;475(1):61-4. PMID:10854859[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pedersen LC, Petrotchenko EV, Negishi M. Crystal structure of SULT2A3, human hydroxysteroid sulfotransferase. FEBS Lett. 2000 Jun 9;475(1):61-4. PMID:10854859
