CINECA IRIS Institutional Research Information System
IRIS è la soluzione IT che facilita la raccolta e la gestione dei dati relativi alle attività e ai prodotti della ricerca. Fornisce a ricercatori, amministratori e valutatori gli strumenti per monitorare i risultati della ricerca, aumentarne la visibilità e allocare in modo efficace le risorse disponibili.
EnglishThe conformation of the bound glutathione (GSH) in the active site of the human glutathione transferase P1-1 (EC 2.5.1.18) has been studied by transferred NOE measurements and compared with those obtained by X-ray diffraction data. Two-dimensional TRNOESY and TRROESY experiments have been performed under fast-exchange conditions. The family of GSH conformers, compatible with TRNOE distance constraints, shows a backbone structure very similar to the crystal model. Interesting differences have been found in the side chain regions. After restrained energy minimization of a representative NMR conformer in the active site, the sulfur atom is not found in hydrogen-bonding distance of the hydroxyl group of Tyr 7. This situation is similar to the one observed in an "atypical" crystal complex grown at low pH and low temperature. The NMR conformers display also a poorly defined structure of the glutamyl moiety, and the presence of an unexpected intermolecular NOE could indicate a different interaction of this substrate portion with the G-site. The NMR data seem to provide a snapshot of GSH in a precomplex where the GSH glutamyl end is bound in a different fashion. The existence of this precomplex is supported by pre-steady-state kinetic experiments [Caccuri, A. M., Lo Bello, M., Nuccetelli, M., Nicotra, M., Rossi, P., Antonini, G., Federici, G., and Ricci, G. (1998) Biochemistry 37, 3028-3034] and preliminary time-resolved fluorescence data.
Nicotra, M., Paci, M., Sette, M., Oakley, A.J., Parker, M.W., Lo Bello, M., et al. (1998). Solution structure of glutathione bound to human glutathione transferase P1-1: Comparison of NMR measurements with the crystal structure. BIOCHEMISTRY, 37(9), 3020-3027.
| Tipologia: | Articolo su rivista | |
| Citazione: | Nicotra, M., Paci, M., Sette, M., Oakley, A.J., Parker, M.W., Lo Bello, M., et al. (1998). Solution structure of glutathione bound to human glutathione transferase P1-1: Comparison of NMR measurements with the crystal structure. BIOCHEMISTRY, 37(9), 3020-3027. | |
| IF: | Con Impact Factor ISI | |
| Lingua: | English | |
| Settore Scientifico Disciplinare: | Settore BIO/10 | |
| Revisione (peer review): | Sì, ma tipo non specificato | |
| Tipo: | Articolo | |
| Rilevanza: | Rilevanza internazionale | |
| Digital Object Identifier (DOI): | http://dx.doi.org/10.1021/bi971902o | |
| Stato di pubblicazione: | Pubblicato | |
| Data di pubblicazione: | 1998 | |
| Titolo: | Solution structure of glutathione bound to human glutathione transferase P1-1: Comparison of NMR measurements with the crystal structure | |
| Autori: | ||
| Autori: | Nicotra, M; Paci, M; Sette, M; Oakley, AJ; Parker, MW; Lo Bello, M; Caccuri, AM; Federici, G; Ricci, G | |
| Appare nelle tipologie: | 01 - Articolo su rivista |
File in questo prodotto:
Copyright © 2021