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Titolo:
Structures of tryparedoxins revealing interaction with trypanothione
Autore:
Hofmann, B; Budde, H; Bruns, K; Guerrero, SA; Kalisz, HM; Menge, U; Montemartini, M; Nogoceke, E; Steinert, P; Wissing, JB; Flohe, L; Hecht, HJ;
Indirizzi:
Tech Univ Braunschweig, Dept Biochem, D-38124 Braunschweig, Germany Tech Univ Braunschweig Braunschweig Germany D-38124 raunschweig, Germany Natl Ctr Biotechnol GBF, Dept Mol Struct Res, D-38124 Braunschweig, Germany Natl Ctr Biotechnol GBF Braunschweig Germany D-38124 aunschweig, Germany
Titolo Testata:
BIOLOGICAL CHEMISTRY
fascicolo: 3, volume: 382, anno: 2001,
pagine: 459 - 471
SICI:
1431-6730(200103)382:3<459:SOTRIW>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
MITOCHONDRIAL THIOREDOXIN REDUCTASE; DEPENDENT PEROXIDASE SYSTEM; CRITHIDIA-FASCICULATA; CRYSTAL-STRUCTURE; TRYPANOSOMA-CRUZI; ANGSTROM RESOLUTION; ACTIVE-SITE; FUNCTIONAL-CHARACTERIZATION; GLUTATHIONE-PEROXIDASE; 2-CYS PEROXIREDOXIN;
Keywords:
enzyme-substrate interaction; site-directed mutagenesis; thioredoxin; trypanothione; tryparedoxin; X-ray structure;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
66
Recensione:
Indirizzi per estratti:
Indirizzo: Flohe, L Tech Univ Braunschweig, Dept Biochem, Mascheroder Weg 1, D-38124 Braunschweig, Germany Tech Univ Braunschweig Mascheroder Weg 1 Braunschweig Germany D-38124
Citazione:
B. Hofmann et al., "Structures of tryparedoxins revealing interaction with trypanothione", BIOL CHEM, 382(3), 2001, pp. 459-471

Abstract

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, CfTXN1 H6; reduced and oxidised CfTXN2, and an alternative substratederivative 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 N-1-glutathionyl residue of trypanothione, as evidenced by thestructure of N-1-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 N-1-glutathionyl-spermidine binding in the CfTXN2H6-Cys44Ser structure.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/03/20 alle ore 23:23:15