View source for 3zbu


==Ferredoxin-NADP Reductase Mutant with SER 80 Replaced by ALA (S80A)==
<StructureSection load='3zbu' size='340' side='right'caption='[[3zbu]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3zbu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Nostoc_sp._PCC_7119 Nostoc sp. PCC 7119]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZBU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZBU 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]] 1.89&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3zbu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zbu OCA], [https://pdbe.org/3zbu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zbu RCSB], [https://www.ebi.ac.uk/pdbsum/3zbu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zbu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FENR_NOSSO FENR_NOSSO] 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:24200908</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3zbu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Nostoc sp. PCC 7119]]
[[Category: Herguedas B]]
[[Category: Hervas M]]
[[Category: Martinez-Julvez M]]
[[Category: Medina M]]
[[Category: Navarro JA]]
[[Category: Sanchez-Azqueta A]]