1OKD

NMR-structure of tryparedoxin 1

1OKD の概要

• エントリーDOI: 10.2210/pdb1okd/pdb
• 関連するPDBエントリー: 1EWX 1EZK 1O7U 1O85 1O8W 1O8X 1QK8
• 分子名称: TRYPAREDOXIN 1 (1 entity in total)
• 機能のキーワード: electron transport, tryparedoxin, trypanosomatids, nmr spectroscopy
• 由来する生物種: Crithidia fasciculata
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17569.78

構造登録者

Krumme, D.,Budde, H.,Hecht, H.-J.,Menge, U.,Ohlenschlager, O.,Ross, A.,Wissing, J.,Wray, V.,Flohe, L. (登録日: 2003-07-22, 公開日: 2003-08-28, 最終更新日: 2024-10-16)

主引用文献

Krumme, D.,Budde, H.,Hecht, H.J.,Menge, U.,Ohlenschlager, O.,Ross, A.,Wissing, J.,Wray, V.,Flohe, L.
NMR studies of the interaction of tryparedoxin with redox-inactive substrate homologues.
Biochemistry, 42:14720-14728, 2003

PubMed Abstract: Tryparedoxins (TXNs) are trypanothione-dependent peroxiredoxin oxidoreductases involved in hydroperoxide detoxification that have been shown to determine virulence in trypanosomatids. The structure of (15)N,(13)C-doubly-labeled, C-terminally-His-tagged tryparedoxin 1 from Crithidia fasciculata (Cf TXN1) was elucidated by three-dimensional NMR spectroscopy. Global folding was found to be similar to the crystal structure, but regions near the active site, especially the onset of helix alpha1 with the redox-active Cys 43 and helix alpha2 relevant to substrate binding, were less well defined in solution. The redox-inactive inhibitory substrate analogue N(1),N(8)-bis(ophthalmyl)spermidine was used to study the substrate/TXN interaction by two-dimensional (1)H,(15)N NMR spectroscopy. The NMR data complemented by molecular modeling revealed several alternative modes of ligand binding. The results confirm and extend the concept of TXN action and specificity derived from X-ray analysis and site-directed mutagenesis and thus improve the rational basis for inhibitor design.

PubMed: 14674746
DOI: 10.1021/bi030112d

実験手法

SOLUTION NMR