5X2B

Crystal structure of mouse sulfotransferase SULT7A1 complexed with PAP

5X2B の概要

• エントリーDOI: 10.2210/pdb5x2b/pdb
• 分子名称: Sulfotransferase, ADENOSINE-3'-5'-DIPHOSPHATE, CALCIUM ION, ... (7 entities in total)
• 機能のキーワード: transferase
• 由来する生物種: Mus musculus (Mouse); 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 397615.47

構造登録者

Kanekiyo, M.,Teramoto, T.,Kakuta, Y. (登録日: 2017-01-31, 公開日: 2018-03-28, 最終更新日: 2025-03-19)

主引用文献

Kurogi, K.,Sakakibara, Y.,Hashiguchi, T.,Kakuta, Y.,Kanekiyo, M.,Teramoto, T.,Fukushima, T.,Bamba, T.,Matsumoto, J.,Fukusaki, E.,Kataoka, H.,Suiko, M.
A new type of sulfation reaction: C -sulfonation for alpha , beta-unsaturated carbonyl groups by a novel sulfotransferase SULT7A1.
Pnas Nexus, 3:pgae097-pgae097, 2024

PubMed Abstract: Cytosolic sulfotransferases (SULTs) are cytosolic enzymes that catalyze the transfer of sulfonate group to key endogenous compounds, altering the physiological functions of their substrates. SULT enzymes catalyze the -sulfonation of hydroxy groups or -sulfonation of amino groups of substrate compounds. In this study, we report the discovery of -sulfonation of α,β-unsaturated carbonyl groups mediated by a new SULT enzyme, SULT7A1, and human SULT1C4. Enzymatic assays revealed that SULT7A1 is capable of transferring the sulfonate group from 3'-phosphoadenosine 5'-phosphosulfate to the α-carbon of α,β-unsaturated carbonyl-containing compounds, including cyclopentenone prostaglandins as representative endogenous substrates. Structural analyses of SULT7A1 suggest that the -sulfonation reaction is catalyzed by a novel mechanism mediated by His and Cys residues in the active site. Ligand-activity assays demonstrated that sulfonated 15-deoxy prostaglandin J exhibits antagonist activity against the prostaglandin receptor EP2 and the prostacyclin receptor IP. Modification of α,β-unsaturated carbonyl groups via the new prostaglandin-sulfonating enzyme, SULT7A1, may regulate the physiological function of prostaglandins in the gut. Discovery of -sulfonation of α,β-unsaturated carbonyl groups will broaden the spectrum of potential substrates and physiological functions of SULTs.

PubMed: 38487162
DOI: 10.1093/pnasnexus/pgae097

実験手法

X-RAY DIFFRACTION (2.08 Å)