3zc3: Difference between revisions
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== | ==FERREDOXIN-NADP REDUCTASE (MUTATION S80A) COMPLEXED WITH NADP BY COCRYSTALLIZATION== | ||
[[3zc3]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZC3 OCA]. | <StructureSection load='3zc3' size='340' side='right'caption='[[3zc3]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3zc3]] is a 2 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=3ZC3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZC3 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]] 2.3Å</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=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=3zc3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zc3 OCA], [https://pdbe.org/3zc3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zc3 RCSB], [https://www.ebi.ac.uk/pdbsum/3zc3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zc3 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> | |||
<ref | |||
[[Category: Herguedas | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
[[Category: Hervas | </div> | ||
[[Category: Hurtado-Guerrero | <div class="pdbe-citations 3zc3" style="background-color:#fffaf0;"></div> | ||
[[Category: Martinez-Julvez | == References == | ||
[[Category: Medina | <references/> | ||
[[Category: Navarro | __TOC__ | ||
[[Category: Sanchez-Azqueta | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Nostoc sp. PCC 7119]] | |||
[[Category: Herguedas B]] | |||
[[Category: Hervas M]] | |||
[[Category: Hurtado-Guerrero R]] | |||
[[Category: Martinez-Julvez M]] | |||
[[Category: Medina M]] | |||
[[Category: Navarro JA]] | |||
[[Category: Sanchez-Azqueta A]] | |||
Latest revision as of 13:58, 20 December 2023
FERREDOXIN-NADP REDUCTASE (MUTATION S80A) COMPLEXED WITH NADP BY COCRYSTALLIZATIONFERREDOXIN-NADP REDUCTASE (MUTATION S80A) COMPLEXED WITH NADP BY COCRYSTALLIZATION
Structural highlights
FunctionPublication Abstract from PubMedFerredoxin-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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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