4bpr

FERREDOXIN-NADP REDUCTASE MUTANT WITH TYR 79 REPLACED BY PHE (Y79F)FERREDOXIN-NADP REDUCTASE MUTANT WITH TYR 79 REPLACED BY PHE (Y79F)

Structural highlights 4bpr is a 1 chain structure with sequence from Anabaena sp.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: , , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FENR_NOSSO Publication Abstract from PubMed Ferredoxin-NADP+ reductase (FNR) catalyses the production of NADPH in photosynthetic organisms, where its FAD cofactor takes two electrons from two reduced ferredoxin (Fd) molecules in two sequential steps, and transfers them to NADP+ in a single hydride transfer (HT) step. Despite the good knowledge of this catalytic machinery, additional roles can still be envisaged for already reported key residues, and new features are added to residues not previously identified as having a particular role in the mechanism. Here, we analyse for the first time the role of Ser59 in Anabaena FNR, a residue suggested by recent theoretical simulations as putatively involved in competent binding of the coenzyme in the active site by cooperating with Ser80. We show that Ser59 indirectly modulates the geometry of the active site, the interaction with substrates and the electronic properties of the isoalloxazine ring, and in consequence the electron transfer (ET) and HT processes. Additionally, we revise the role of Tyr79 and Ser80, previously investigated in homologous enzymes from plants. Our results probe that the active site of FNR is tuned by a H-bond network that involves the side-chains of these residues and that results to critical optimal substrate binding, exchange of electrons and, particularly, competent disposition of the C4n (hydride acceptor/donor) of the nicotinamide moiety of the coenzyme during the reversible HT event. A hydrogen bond network in the active site of Anabaena ferredoxin-NADP reductase modulates its catalytic efficiency.,Sanchez-Azqueta A, Herguedas B, Hurtado-Guerrero R, Hervas M, Navarro JA, Martinez-Julvez M, Medina M Biochim Biophys Acta. 2013 Nov 4. pii: S0005-2728(13)00180-1. doi:, 10.1016/j.bbabio.2013.10.010. PMID:24200908 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 4bpr, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image