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http://purl.uniprot.org/citations/11347894http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11347894http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11347894http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/11347894http://purl.org/dc/terms/identifier"doi:10.1515/BC.2001.056"xsd:string
http://purl.uniprot.org/citations/11347894http://purl.org/dc/terms/identifier"doi:10.1515/bc.2001.056"xsd:string
http://purl.uniprot.org/citations/11347894http://purl.uniprot.org/core/author"Kalisz H.M."xsd:string
http://purl.uniprot.org/citations/11347894http://purl.uniprot.org/core/author"Kalisz H.M."xsd:string
http://purl.uniprot.org/citations/11347894http://purl.uniprot.org/core/author"Montemartini M."xsd:string
http://purl.uniprot.org/citations/11347894http://purl.uniprot.org/core/author"Montemartini M."xsd:string
http://purl.uniprot.org/citations/11347894http://purl.uniprot.org/core/author"Flohe L."xsd:string
http://purl.uniprot.org/citations/11347894http://purl.uniprot.org/core/author"Flohe L."xsd:string
http://purl.uniprot.org/citations/11347894http://purl.uniprot.org/core/author"Guerrero S.A."xsd:string
http://purl.uniprot.org/citations/11347894http://purl.uniprot.org/core/author"Guerrero S.A."xsd:string
http://purl.uniprot.org/citations/11347894http://purl.uniprot.org/core/author"Menge U."xsd:string
http://purl.uniprot.org/citations/11347894http://purl.uniprot.org/core/author"Menge U."xsd:string
http://purl.uniprot.org/citations/11347894http://purl.uniprot.org/core/author"Budde H."xsd:string
http://purl.uniprot.org/citations/11347894http://purl.uniprot.org/core/author"Budde H."xsd:string
http://purl.uniprot.org/citations/11347894http://purl.uniprot.org/core/author"Hecht H.J."xsd:string
http://purl.uniprot.org/citations/11347894http://purl.uniprot.org/core/author"Hecht H.J."xsd:string
http://purl.uniprot.org/citations/11347894http://purl.uniprot.org/core/author"Hofmann B."xsd:string
http://purl.uniprot.org/citations/11347894http://purl.uniprot.org/core/author"Hofmann B."xsd:string
http://purl.uniprot.org/citations/11347894http://purl.uniprot.org/core/author"Bruns K."xsd:string
http://purl.uniprot.org/citations/11347894http://purl.uniprot.org/core/author"Bruns K."xsd:string
http://purl.uniprot.org/citations/11347894http://purl.uniprot.org/core/author"Wissing J.B."xsd:string
http://purl.uniprot.org/citations/11347894http://purl.uniprot.org/core/author"Wissing J.B."xsd:string