2A3R

Crystal Structure of Human Sulfotransferase SULT1A3 in Complex with Dopamine and 3-Phosphoadenosine 5-Phosphate

2A3R の概要

• エントリーDOI: 10.2210/pdb2a3r/pdb
• 分子名称: Monoamine-sulfating phenol sulfotransferase, ADENOSINE-3'-5'-DIPHOSPHATE, L-DOPAMINE, ... (4 entities in total)
• 機能のキーワード: sult1a3, dopamine, complex, sulfotransferase, transferase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 69635.01

構造登録者

Lu, J.H.,Li, H.T.,Liu, M.C.,Zhang, J.P.,Li, M.,An, X.M.,Chang, W.R. (登録日: 2005-06-26, 公開日: 2005-08-30, 最終更新日: 2023-10-25)

主引用文献

Lu, J.H.,Li, H.T.,Liu, M.C.,Zhang, J.P.,Li, M.,An, X.M.,Chang, W.R.
Crystal structure of human sulfotransferase SULT1A3 in complex with dopamine and 3'-phosphoadenosine 5'-phosphate
Biochem.Biophys.Res.Commun., 335:417-423, 2005

PubMed Abstract: The human sulfotransferase, SULT1A3, catalyzes specifically the sulfonation of monoamines such as dopamine, epinephrine, and norepinephrine. SULT1A3 also has a unique 3,4-dihydroxyphenylalanine (Dopa)/tyrosine-sulfating activity that is preferentially toward their D-form enantiomers and can be stimulated dramatically by Mn2+. To further our understanding of the molecular basis for the unique substrate specificity of this enzyme, we solved the crystal structure of human SULT1A3, complexed with dopamine and 3'-phosphoadenosine 5'-phosphate, at 2.6 A resolution and carried out autodocking analysis with D-Dopa. The structure of SULT1A3 enzyme-ligand complex clearly showed that residue Glu146 can form electrostatic interaction with dopamine and may play a pivotal role in the stereoselectivity and sulfating activity. On the other hand, residue Asp86 appeared to be critical to the Mn2+-stimulation of the Dopa/tyrosine-sulfating activity of SULT1A3, in addition to a supporting role in the stereoselectivity and sulfating activity.

PubMed: 16083857
DOI: 10.1016/j.bbrc.2005.07.091

実験手法

X-RAY DIFFRACTION (2.6 Å)