1w87

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[[Image:1w87.png|left|200px]]
 
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==FERREDOXIN-NADP REDUCTASE (MUTATION: Y 303 W) COMPLEXED WITH NADP BY COCRYSTALLIZATION==
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The line below this paragraph, containing "STRUCTURE_1w87", creates the "Structure Box" on the page.
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<StructureSection load='1w87' size='340' side='right'caption='[[1w87]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1w87]] 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=1W87 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W87 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
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<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=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
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{{STRUCTURE_1w87| PDB=1w87 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1w87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w87 OCA], [https://pdbe.org/1w87 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w87 RCSB], [https://www.ebi.ac.uk/pdbsum/1w87 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w87 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FENR_NOSSO FENR_NOSSO]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w8/1w87_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1w87 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Ferredoxin-NADP+ reductase (FNR) catalyzes the reduction of NADP+ to NADPH in an overall reversible reaction, showing some differences in the mechanisms between cyanobacterial and higher plant FNRs. During hydride transfer it is proposed that the FNR C-terminal Tyr is displaced by the nicotinamide. Thus, this C-terminal Tyr might be involved not only in modulating the flavin redox properties, as already shown, but also in nicotinamide binding and hydride transfer. FNR variants from the cyanobacterium Anabaena in which the C-terminal Tyr has been replaced by Trp, Phe, or Ser have been produced. All FNR variants show enhanced NADP+ and NAD+ binding, especially Tyr303Ser, which correlates with a noticeable improvement of NADH-dependent reactions. Nevertheless, the Tyr303Ser variant shows a decrease in the steady-state kcat value with NADPH. Fast kinetic analysis of the hydride transfer shows that the low efficiency observed for this mutant FNR under steady-state conditions is not due to a lack of catalytic ability but rather to the strong enzyme-coenzyme interaction. Three-dimensional structures for Tyr303Ser and Tyr303Trp variants and its complexes with NADP+ show significant differences between plant and cyanobacterial FNRs. Our results suggest that modulation of coenzyme affinity is highly influenced by the strength of the C-terminus-FAD interaction and that subtle changes between plant and cyanobacterial structures are able to modify the energy of that interaction. Additionally, it is shown that the C-terminal Tyr of FNR lowers the affinity for NADP+/H to levels compatible with steady-state turnover during the catalytic cycle, but it is not involved in the hydride transfer itself.
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===FERREDOXIN-NADP REDUCTASE (MUTATION: Y 303 W) COMPLEXED WITH NADP BY COCRYSTALLIZATION===
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C-terminal tyrosine of ferredoxin-NADP+ reductase in hydride transfer processes with NAD(P)+/H.,Tejero J, Perez-Dorado I, Maya C, Martinez-Julvez M, Sanz-Aparicio J, Gomez-Moreno C, Hermoso JA, Medina M Biochemistry. 2005 Oct 18;44(41):13477-90. PMID:16216071<ref>PMID:16216071</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_16216071}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1w87" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16216071 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16216071}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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[[1w87]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W87 OCA].
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[[Category: Nostoc sp. PCC 7119]]
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[[Category: Hermoso JA]]
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==Reference==
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[[Category: Maya C]]
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<ref group="xtra">PMID:16216071</ref><ref group="xtra">PMID:12079352</ref><references group="xtra"/>
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[[Category: Perez-Dorado I]]
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[[Category: Anabaena sp.]]
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[[Category: Hermoso, J A.]]
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[[Category: Maya, C.]]
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[[Category: Perez-Dorado, I.]]
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[[Category: 3d-structure]]
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[[Category: Fad]]
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[[Category: Flavoprotein]]
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[[Category: Fnr]]
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[[Category: Nadp]]
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[[Category: Nadp reductase]]
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[[Category: Oxidoreductase]]
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[[Category: Phycobilisome]]
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[[Category: Thylakoid]]
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Current revision

FERREDOXIN-NADP REDUCTASE (MUTATION: Y 303 W) COMPLEXED WITH NADP BY COCRYSTALLIZATION

PDB ID 1w87

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