5vw2 | pdb_00005vw2

NADPH soak of Y316S mutant of corn root ferredoxin:NADP+ reductase

spinqualitylabelsall models 5vw2, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5vw2 is a 1 chain structure with sequence from Maize. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, FDA, MG, NAP Related: 5vw3, 5vw4, 5vw5, 5vw6, 5vw8, 5vw7, 5vwb, 5vw9, 5vwa Activity: Ferredoxin--NADP(+) reductase, with EC number 1.18.1.2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Ferredoxin-NADP+ reductase (FNR) is an FAD-containing enzyme best known for catalyzing the transfer of electrons from ferredoxin (Fd) to NADP+ to make NADPH during photosynthesis. It is also the prototype for a broad enzyme superfamily, including the NADPH oxidases (NOXs) that all catalyze similar FAD-enabled electron transfers between NAD(P)H and one-electron carriers. Here we define further mechanistic details of the NAD(P)H This article is protected by copyright. All rights reserved. right harpoon over left harpoon FAD hydride-transfer step of the reaction based on spectroscopic studies and high resolution (~1.5 A) crystallographic views of the nicotinamide-flavin interaction in crystals of corn root FNR Tyr316Ser and Tyr316Ala variants soaked with either nicotinamide, NADP+ , or NADPH. The spectra obtained from FNR crystal complexes match those seen in solution and the complexes reveal active site packing interactions and patterns of covalent distortion of the FAD that imply significant active site compression that would favor catalysis. Furthermore, anisotropic B-factors show that the mobility of the C4 atom of the nicotinamide in the FNR:NADP+ complex has a directionality matching that expected for boat-like excursions of the nicotinamide ring thought to enhance hydride transfer. Arguments are made for the relevance of this binding mode to catalysis, and specific consideration is given to how the results extrapolate to provide insight to structure-function relations for the membrane-bound NOX enzymes for which little structural information has been available. This article is protected by copyright. All rights reserved. High resolution studies of hydride transfer in the ferredoxin:NADP+ reductase superfamily.,Kean KM, Carpenter RA, Pandini V, Zanetti G, Hall AR, Faber R, Aliverti A, Karplus PA FEBS J. 2017 Aug 7. doi: 10.1111/febs.14190. PMID:28783258 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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