1ezk: Difference between revisions

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[[Image:1ezk.jpg|left|200px]]
{{Seed}}
[[Image:1ezk.png|left|200px]]


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{{STRUCTURE_1ezk|  PDB=1ezk  |  SCENE=  }}  
{{STRUCTURE_1ezk|  PDB=1ezk  |  SCENE=  }}  


'''Crystal structure of recombinant tryparedoxin I'''
===Crystal structure of recombinant tryparedoxin I===




==Overview==
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Tryparedoxins (TXNs) catalyse the reduction of peroxiredoxin-type peroxidases by the bis-glutathionyl derivative of spermidine, trypanothione, and are relevant to hydroperoxide detoxification and virulence of trypanosomes. The 3D-structures of the following tryparedoxins are presented: authentic tryparedoxin1 of Crithidia fasciculata, CfTXN1; the his-tagged recombinant protein, CfTXN1H6; reduced and oxidised CfTXN2, and an alternative substrate derivative of the mutein CfTXN2H6-Cys44Ser. Cys41 (Cys40 in TXN1) of the active site motif 40-WCPPCR-45 proved to be the only solvent-exposed redox active residue in CfTXN2. In reduced TXNs, its nucleophilicity is increased by a network of hydrogen bonds. In oxidised TXNs it can be attacked by the thiol of the 1N-glutathionyl residue of trypanothione, as evidenced by the structure of 1N-glutathionylspermidine-derivatised CfTXN2H6-Cys44Ser. Modelling suggests Arg45 (44), Glu73 (72), the Ile110 (109) cis-Pro111 (110)-bond and Arg129 (128) to be involved in the binding of trypanothione to CfTXN2 (CfTXN1). The model of TXN-substrate interaction is consistent with functional characteristics of known and newly designed muteins (CfTXN2H6-Arg129Asp and Glu73Arg) and the 1N-glutathionyl-spermidine binding in the CfTXN2H6-Cys44Ser structure.
The line below this paragraph, {{ABSTRACT_PUBMED_11347894}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_11347894}}


==About this Structure==
==About this Structure==
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[[Category: Singh, M.]]
[[Category: Singh, M.]]
[[Category: Electron transport]]
[[Category: Electron transport]]
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