Crystallization and preliminary crystallographic results of apo and complex forms of human dehydroepiandrosterone sulfotransferase

Abstract

Dehydroepiandrosterone sulfotransferase converts dehydroepiandrosterone (DHEA) and some other steroids to their sulfonated forms. The human enzyme has been crystallized in the presence of substrate (DHEA) alone, in the presence of substrate and non-sulfated cofactor analogue (PAP) and in the absence of both substrate and PAP in our laboratory, with data sets collected at a synchrotron source. The crystals of the uncomplexed form belong to the orthorhombic space group C222(1), with unit-cell parameters a = 85.26, b = 87.69, c = 108.20 A and data 99.2% complete to 2.35 A resolution. The DHEA complex crystallizes in the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 74.46, b = 127.49, c = 44.59 A and data 92.9% complete to 2.15 A resolution. The ternary complex crystallizes in the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 62.25, b = 87.28, c = 138.86 A and data 98.6% complete to 2.50 A resolution. Preliminary molecular-replacement solutions indicate significant variations in dimer formation.