1gjr
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The flavoenzyme ferredoxin-NADP+ reductase (FNR) catalyses the production | + | 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. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Gomez-Moreno, C.]] | [[Category: Gomez-Moreno, C.]] | ||
| - | [[Category: Hermoso, J | + | [[Category: Hermoso, J A.]] |
[[Category: Mayoral, T.]] | [[Category: Mayoral, T.]] | ||
[[Category: Medina, M.]] | [[Category: Medina, M.]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:50:51 2008'' |
Revision as of 10:50, 21 February 2008
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FERREDOXIN-NADP+ REDUCTASE COMPLEXED WITH NADP+ BY COCRYSTALLIZATION
Overview
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.
About this Structure
1GJR is a Single protein structure of sequence from Anabaena sp. with and as ligands. Active as Ferredoxin--NADP(+) reductase, with EC number 1.18.1.2 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Mechanism of coenzyme recognition and binding revealed by crystal structure analysis of ferredoxin-NADP+ reductase complexed with NADP+., Hermoso JA, Mayoral T, Faro M, Gomez-Moreno C, Sanz-Aparicio J, Medina M, J Mol Biol. 2002 Jun 21;319(5):1133-42. PMID:12079352
Page seeded by OCA on Thu Feb 21 12:50:51 2008
Categories: Anabaena sp. | Ferredoxin--NADP(+) reductase | Single protein | Gomez-Moreno, C. | Hermoso, J A. | Mayoral, T. | Medina, M. | Sanz-Aparicio, J. | FAD | NAP | Fad | Flavoprotein | Fnr | Nadp | Nadp reductase | Oxidoreductase
