1OV4

Crystal structure of human DHEA-ST complexed with androsterone

1OV4 の概要

• エントリーDOI: 10.2210/pdb1ov4/pdb
• 関連するPDBエントリー: 1EFH 1J99
• 分子名称: Alcohol sulfotransferase, SULFATE ION, (3Beta,5alpha)-3-Hydroxyandrostan-17-one, ... (4 entities in total)
• 機能のキーワード: alpha/beta fold, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q06520
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35103.21

構造登録者

Chang, H.J.,Shi, R.,Rhese, P.,Lin, S.X. (登録日: 2003-03-25, 公開日: 2004-02-17, 最終更新日: 2023-08-16)

主引用文献

Chang, H.J.,Shi, R.,Rehse, P.,Lin, S.X.
Identifying androsterone (ADT) as a cognate substrate for human dehydroepiandrosterone sulfotransferase (DHEA-ST) important for steroid homeostasis: structure of the enzyme-ADT complex.
J.Biol.Chem., 279:2689-2696, 2004

PubMed Abstract: In steroid biosynthesis, human dehydroepiandrosterone sulfotransferase (DHEA-ST) in the adrenals has been reported to catalyze the transfer of the sulfonate group from 3'-phosphoadenosine-5'-phosphosulfate to dehydroepiandrosterone (DHEA). DHEA and its sulfate play roles as steroid precursors; however, the role of the enzyme in the catabolism of androgens is poorly understood. Androsterone sulfate is clinically recognized as one of the major androgen metabolites found in urine. Here it is demonstrated that this enzyme recognizes androsterone (ADT) as a cognate substrate with similar kinetics but a 2-fold specificity and stronger substrate inhibition than DHEA. The structure of human DHEA-ST in complex with ADT has been solved at 2.7 A resolution, confirming ADT recognition. Structural analysis has revealed the binding mode of ADT differs from that of DHEA, despite the similarity of the overall structure between the ADT and the DHEA binary complexes. Our results identify that this human enzyme is an ADT sulfotransferase as well as a DHEA sulfotransferase, implying an important role in steroid homeostasis for the adrenals and liver.

PubMed: 14573603
DOI: 10.1074/jbc.M310446200

実験手法

X-RAY DIFFRACTION (2.7 Å)