5TIV

Schistosoma haematobium (Blood Fluke) Sulfotransferase

5TIV の概要

• エントリーDOI: 10.2210/pdb5tiv/pdb
• 関連するPDBエントリー: 5TIW 5TIX 5TIY 5TIZ
• 分子名称: Sulfotransferase, ADENOSINE-3'-5'-DIPHOSPHATE, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total)
• 機能のキーワード: sulfotransferase, parasite, helminth, transferase
• 由来する生物種: Schistosoma haematobium (Blood fluke)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29811.91

構造登録者

Taylor, A.B.,Hart, P.J. (登録日: 2016-10-03, 公開日: 2017-05-31, 最終更新日: 2023-10-04)

主引用文献

Taylor, A.B.,Roberts, K.M.,Cao, X.,Clark, N.E.,Holloway, S.P.,Donati, E.,Polcaro, C.M.,Pica-Mattoccia, L.,Tarpley, R.S.,McHardy, S.F.,Cioli, D.,LoVerde, P.T.,Fitzpatrick, P.F.,Hart, P.J.
Structural and enzymatic insights into species-specific resistance to schistosome parasite drug therapy.
J. Biol. Chem., 292:11154-11164, 2017

PubMed Abstract: The antischistosomal prodrug oxamniquine is activated by a sulfotransferase (SULT) in the parasitic flatworm Of the three main human schistosome species, only is sensitive to oxamniquine therapy despite the presence of SULT orthologs in and The reason for this species-specific drug action has remained a mystery for decades. Here we present the crystal structures of and SULTs, including SULT in complex with oxamniquine. We also examined the activity of the three enzymes ; surprisingly, all three are active toward oxamniquine, yet we observed differences in catalytic efficiency that implicate kinetics as the determinant for species-specific toxicity. These results provide guidance for designing oxamniquine derivatives to treat infection caused by all species of schistosome to combat emerging resistance to current therapy.

PubMed: 28536265
DOI: 10.1074/jbc.M116.766527

実験手法

X-RAY DIFFRACTION (1.43 Å)