View source for 5vw7


==NADPH soak of Y316A mutant of corn root ferredoxin:NADP+ reductase==
<StructureSection load='5vw7' size='340' side='right'caption='[[5vw7]], [[Resolution|resolution]] 1.61&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5vw7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VW7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VW7 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.608&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FDA:DIHYDROFLAVINE-ADENINE+DINUCLEOTIDE'>FDA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5vw7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vw7 OCA], [https://pdbe.org/5vw7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vw7 RCSB], [https://www.ebi.ac.uk/pdbsum/5vw7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vw7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B4G043_MAIZE B4G043_MAIZE] 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:28783258</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5vw7" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Zea mays]]
[[Category: Carpenter RA]]
[[Category: Hall AR]]
[[Category: Karplus PA]]
[[Category: Kean KM]]