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  The Structure of Trypanosoma cruzitrypanothione Reductase in the Oxidized and NADPH Reduced State

Lantwin, C. B., Schlichting, I., Kabsch, W., Pai, E. F., & Krauth-Siegel, R. L. (1994). The Structure of Trypanosoma cruzitrypanothione Reductase in the Oxidized and NADPH Reduced State. Proteins: Structure, Function, and Bioinformatics, 18(2), 161-173. doi:10.1002/prot.340180208.

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Lantwin, Christina B.1, Author              
Schlichting, Ilme1, 2, Author              
Kabsch, Wolfgang1, 2, Author              
Pai, Emil F., Author
Krauth-Siegel, R. Luise, Author
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1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 Abstract: The three-dimensional structure of trypanothione reductase (TR) (EC 1.6.4.8) from Trypanosoma cruzi has been solved at 0.33 nm resolution by molecular replacement using the structure of C. fasciculata TR as a starting model. Elucidation of the T. cruzi TR structure represents the first step in the rational design of a drug against Chagas' disease. The structure of T. cruzi TR is compared with those of C. fasciculata TR as well as human and E. coli glutathione reductase (GR). In the FAD-binding domain, TR has two insertions, each about 10 residues long, which do not occur in GR. The first one is a rigid loop stabilizing the position of helix 91–117 which is responsible for the wider active site of TR as compared to GR. The second insertion does not occur where it is predicted by sequence alignment; rather the residues extend three strands of the 4-stranded β-sheet by one or two residues each. This increases the number of hydrogen bonds within the sheet structure. The structure of the NADPH.TR complex has been solved at 0.33 nm resolution. The nicotinamide ring is sandwiched between the flavin ring and the side chain of Phe-198 which undergoes the same conformational change upon coenzyme binding as Tyr-197 in GR. In addition to Arg-222 and Arg-228, which are conserved in TR and GR, Tyr-221—the last residue of the second β-sheet strand of the βαβ dinucleotide binding fold—is in hydrogen bonding distance to the 2′ phosphate group of NADPH.

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Language(s): eng - English
 Dates: 1993-07-061993-09-212004-02-031994-02
 Publication Status: Published in print
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 Rev. Type: Peer
 Identifiers: eDoc: 665163
DOI: 10.1002/prot.340180208
Other: 6906
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Title: Proteins: Structure, Function, and Bioinformatics
Source Genre: Journal
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Publ. Info: New York, NY : John Wiley & Sons
Pages: - Volume / Issue: 18 (2) Sequence Number: - Start / End Page: 161 - 173 Identifier: ISSN: 0887-3585
CoNE: https://pure.mpg.de/cone/journals/resource/954925553393_1