1EFH

CRYSTAL STRUCTURE OF THE HUMAN HYDROXYSTEROID SULFOTRANSFERASE IN THE PRESENCE OF PAP

Summary for 1EFH

• Entry DOI: 10.2210/pdb1efh/pdb
• Descriptor: HYDROXYSTEROID SULFOTRANSFERASE, ADENOSINE-3'-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: hydroxysteroid, sulfotransferase, dhea, a3p, paps, sult2a3, transferase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 69945.63

Authors

Pedersen, L.C.,Petrotchenko, E.V.,Negishi, M. (deposition date: 2000-02-08, release date: 2000-09-06, Last modification date: 2024-02-07)

Primary citation

Pedersen, L.C.,Petrotchenko, E.V.,Negishi, M.
Crystal structure of SULT2A3, human hydroxysteroid sulfotransferase.
FEBS Lett., 475:61-64, 2000

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.

PubMed: 10854859
DOI: 10.1016/S0014-5793(00)01479-4

Experimental method

X-RAY DIFFRACTION (2.4 Å)