3zbt: Difference between revisions
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<StructureSection load='3zbt' size='340' side='right'caption='[[3zbt]], [[Resolution|resolution]] 1.92Å' scene=''> | <StructureSection load='3zbt' size='340' side='right'caption='[[3zbt]], [[Resolution|resolution]] 1.92Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3zbt]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3zbt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Anabaena_pcc7119 Anabaena pcc7119]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZBT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZBT FirstGlance]. <br> | ||
</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> | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3zbu|3zbu]], [[3zc3|3zc3]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3zbu|3zbu]], [[3zc3|3zc3]]</div></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ferredoxin--NADP(+)_reductase Ferredoxin--NADP(+) reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.1.2 1.18.1.2] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3zbt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zbt OCA], [https://pdbe.org/3zbt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zbt RCSB], [https://www.ebi.ac.uk/pdbsum/3zbt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zbt ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Revision as of 08:41, 10 August 2022
Ferredoxin-NADP Reductase Mutant with SER 59 Replaced by ALA (S59A)Ferredoxin-NADP Reductase Mutant with SER 59 Replaced by ALA (S59A)
Structural highlights
Publication 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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