2ZPT

Crystal structure of mouse sulfotransferase SULT1D1 complex with PAP

2ZPT の概要

• エントリーDOI: 10.2210/pdb2zpt/pdb
• 分子名称: Tyrosine-ester sulfotransferase, ADENOSINE-3'-5'-DIPHOSPHATE, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: sult1d1, catecholamine, sulfotransferase, sulfonation, transferase
• 由来する生物種: Mus musculus (mouse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35647.59

構造登録者

Teramoto, T.,Sakakibara, Y.,Inada, K.,Liu, M.C.,Suiko, M.,Kimura, M.,Kakuta, Y. (登録日: 2008-07-28, 公開日: 2008-11-18, 最終更新日: 2023-11-01)

主引用文献

Teramoto, T.,Sakakibara, Y.,Inada, K.,Kurogi, K.,Liu, M.-C.,Suiko, M.,Kimura, M.,Kakuta, Y.
Crystal structure of mSULT1D1, a mouse catecholamine sulfotransferase
Febs Lett., 582:3909-3914, 2008

PubMed Abstract: In mammals, sulfonation as mediated by specific cytosolic sulfotransferases (SULTs) plays an important role in the homeostasis of dopamine and other catecholamines. To gain insight into the structural basis for dopamine recognition/binding, we determined the crystal structure of a mouse dopamine-sulfating SULT, mouse SULT1D1 (mSULT1D1). Data obtained indicated that mSULT1D1 comprises of a single alpha/beta domain with a five-stranded parallel beta-sheet. In contrast to the structure of the human SULT1A3 (hSULT1A3)-dopamine complex previously reported, molecular modeling and mutational analysis revealed that a water molecule plays a critical role in the recognition of the amine group of dopamine by mSULT1D1. These results imply differences in substrate binding between dopamine-sulfating SULTs from different species.

PubMed: 18977225
DOI: 10.1016/j.febslet.2008.10.035

実験手法

X-RAY DIFFRACTION (1.15 Å)