INVESTIGADORES
CECCARELLI Eduardo Augusto
artículos
Título:
A productive NADP+ binding mode of ferredoxin-NADP + reductase revealed by protein engineering and crystallographic studies
Autor/es:
DENG, Z; ALIVERTI, A; ZANETTI, G; ARAKAKI, A; OTTADO, J; ORELLANO, E; CALCATERRA, N; CECCARELLI, EDUARDO AUGUSTO; CARRILLO, N; KARPLUS, P
Revista:
NATURE STRUCT. BIOL.
Editorial:
Nature Pub. Co
Referencias:
Lugar: Nueva York; Año: 1999 vol. 6 p. 847 - 853
ISSN:
1072-8368
Resumen:
The flavoenzyme ferredoxin?NADP+ reductase (FNR) catalyzes the production of NADPH during photosynthesis. Whereas the structures of FNRs from spinach leaf and a cyanobacterium as well as many of their homologs have been solved, none of these studies has yielded a productive geometry of the flavin?nicotinamide interaction. Here, we show that this failure occurs because nicotinamide binding to wild type FNR involves the energetically unfavorable displacementof the C-terminal Tyr side chain. We used mutants of this residue (Tyr 308) of pea FNR to obtain the structures of productive NADP+ and NADPH complexes. These structures reveal a unique NADP+ binding mode in which the nicotinamide ring is not parallel to the flavin isoalloxazine ring, but lies against it at an angle of ~30°, with the C4 atom 3 Å from the flavin N5 atom.
