1GJR

Ferredoxin-NADP+ Reductase complexed with NADP+ by COCRYSTALLIZATION

Summary for 1GJR

• Entry DOI: 10.2210/pdb1gjr/pdb
• Related: 1B2R 1BJK 1E62 1E63 1E64 1EWY 1H85 1QUE 1QUF
• Descriptor: FERREDOXIN-NADP REDUCTASE, FLAVIN-ADENINE DINUCLEOTIDE, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (4 entities in total)
• Functional Keywords: oxidoreductase, flavoprotein, nadp, fad, fnr, nadp reductase
• Biological source: ANABAENA SP.
• Total number of polymer chains: 1
• Total formula weight: 35701.83

Authors

Hermoso, J.A.,Mayoral, T.,Medina, M.,Sanz-Aparicio, J.,Gomez-Moreno, C. (deposition date: 2001-08-01, release date: 2002-06-27, Last modification date: 2023-12-13)

Primary citation

Hermoso, J.,Mayoral, T.,Faro, M.,Gomez-Moreno, C.,Sanz-Aparicio, J.,Medina, M.
Mechanism of Coenzyme Recognition and Binding Revealed by Crystal Structure Analysis of Ferredoxin-Nadp(+) Reductase Complexed with Nadp(+)
J.Mol.Biol., 319:1133-, 2002

PubMed Abstract: The flavoenzyme ferredoxin-NADP+ reductase (FNR) catalyses the production of NADPH in photosynthesis. The three-dimensional structure of FNR presents two distinct domains, one for binding of the FAD prosthetic group and the other for NADP+ binding. In spite of extensive experiments and different crystallographic approaches, many aspects about how the NADP+ substrate binds to FNR and how the hydride ion is transferred from FAD to NADP+ remain unclear. The structure of an FNR:NADP+ complex from Anabaena has been determined by X-ray diffraction analysis of the cocrystallised units to 2.1 A resolution. Structural perturbation of FNR induced by complex formation produces a narrower cavity in which the 2'-phospho-AMP and pyrophosphate portions of the NADP+ are perfectly bound. In addition, the nicotinamide mononucleotide moiety is placed in a new pocket created near the FAD cofactor with the ribose being in a tight conformation. The crystal structure of this FNR:NADP+ complex obtained by cocrystallisation displays NADP+ in an unusual conformation and can be considered as an intermediate state in the process of coenzyme recognition and binding. Structural analysis and comparison with previously reported complexes allow us to postulate a mechanism which would permit efficient hydride transfer to occur. Besides, this structure gives new insights into the postulated formation of the ferredoxin:FNR:NADP+ ternary complex by prediction of new intermolecular interactions, which could only exist after FNR:NADP+ complex formation. Finally, structural comparison with the members of the broad FNR structural family also provides an explanation for the high specificity exhibited by FNR for NADP+/H versus NAD+/H.

PubMed: 12079352
DOI: 10.1016/S0022-2836(02)00388-1

Experimental method

X-RAY DIFFRACTION (2.1 Å)