1gjr: Difference between revisions
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Revision as of 16:09, 30 October 2007
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FERREDOXIN-NADP+ REDUCTASE COMPLEXED WITH NADP+ BY COCRYSTALLIZATION
OverviewOverview
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 ... [(full description)]
About this StructureAbout this Structure
1GJR is a [Single protein] structure of sequence from [Anabaena sp.] with FAD and NAP as [ligands]. Active as [Ferredoxin--NADP(+) reductase], with EC number [1.18.1.2]. Structure known Active Site: FAD. Full crystallographic information is available from [OCA].
ReferenceReference
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
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