1OKD

NMR-structure of tryparedoxin 1

Summary for 1OKD

• Entry DOI: 10.2210/pdb1okd/pdb
• Related: 1EWX 1EZK 1O7U 1O85 1O8W 1O8X 1QK8
• Descriptor: TRYPAREDOXIN 1 (1 entity in total)
• Functional Keywords: electron transport, tryparedoxin, trypanosomatids, nmr spectroscopy
• Biological source: Crithidia fasciculata
• Total number of polymer chains: 1
• Total formula weight: 17569.78

Authors

Krumme, D.,Budde, H.,Hecht, H.-J.,Menge, U.,Ohlenschlager, O.,Ross, A.,Wissing, J.,Wray, V.,Flohe, L. (deposition date: 2003-07-22, release date: 2003-08-28, Last modification date: 2024-10-16)

Primary citation

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

Experimental method

SOLUTION NMR