1QGA

PEA FNR Y308W MUTANT IN COMPLEX WITH NADP+

Summary for 1QGA

• Entry DOI: 10.2210/pdb1qga/pdb
• Related: 1QFY 1QFZ 1QG0
• Descriptor: PROTEIN (FERREDOXIN:NADP+ REDUCTASE), SULFATE ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (5 entities in total)
• Functional Keywords: flavoenzyme, photosynthesis, electron transfer, hydride transfer, oxidoreductase
• Biological source: Pisum sativum (pea)
• Cellular location: Plastid, chloroplast stroma: P10933
• Total number of polymer chains: 2
• Total formula weight: 72888.18

Authors

Deng, Z.,Aliverti, A.,Zanetti, G.,Arakaki, A.K.,Ottado, J.,Orellano, E.G.,Calcaterra, N.B.,Ceccarelli, E.A.,Carrillo, N.,Karplus, P.A. (deposition date: 1999-04-18, release date: 1999-04-27, Last modification date: 2024-04-03)

Primary citation

Deng, Z.,Aliverti, A.,Zanetti, G.,Arakaki, A.K.,Ottado, J.,Orellano, E.G.,Calcaterra, N.B.,Ceccarelli, E.A.,Carrillo, N.,Karplus, P.A.
A productive NADP+ binding mode of ferredoxin-NADP+ reductase revealed by protein engineering and crystallographic studies.
Nat.Struct.Biol., 6:847-853, 1999

PubMed Abstract: 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 displacement of 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 approximately 30 degrees, with the C4 atom 3 A from the flavin N5 atom.

PubMed: 10467097
DOI: 10.1038/12307

Experimental method

X-RAY DIFFRACTION (2 Å)