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[[Image:1frn.gif|left|200px]]


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==THE INVOLVEMENT OF SER96 IN THE CATALYTIC MECHANISM OF FERREDOXIN-NADP+ REDUCTASE: STRUCTURE-FUNCTION RELATIONSHIP AS STUDIED BY SITE-DIRECTED MUTAGENESIS AND X-RAY CRYSTALLOGRAPHY==
The line below this paragraph, containing "STRUCTURE_1frn", creates the "Structure Box" on the page.
<StructureSection load='1frn' size='340' side='right'caption='[[1frn]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1frn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FRN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FRN FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</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&#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=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
{{STRUCTURE_1frn|  PDB=1frn  |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1frn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1frn OCA], [https://pdbe.org/1frn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1frn RCSB], [https://www.ebi.ac.uk/pdbsum/1frn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1frn ProSAT]</span></td></tr>
 
</table>
'''THE INVOLVEMENT OF SER96 IN THE CATALYTIC MECHANISM OF FERREDOXIN-NADP+ REDUCTASE: STRUCTURE-FUNCTION RELATIONSHIP AS STUDIED BY SITE-DIRECTED MUTAGENESIS AND X-RAY CRYSTALLOGRAPHY'''
== Function ==
 
[https://www.uniprot.org/uniprot/FENR_SPIOL FENR_SPIOL] May play a key role in regulating the relative amounts of cyclic and non-cyclic electron flow to meet the demands of the plant for ATP and reducing power.
 
== Evolutionary Conservation ==
==Overview==
[[Image:Consurf_key_small.gif|200px|right]]
The crystal structure of ferredoxin-NADP+ reductase (FNR) suggests that Ser96 is directly involved in hydride transfer between the isoalloxazine moiety of FAD and the nicotinamide ring of NADP(H). To probe its role, Ser96 has been mutated to valine (S96V) and glycine (S96G). These mutations primarily affected the interaction of the nicotinamide ring with the flavin. Absorbance, fluorescence, and circular dichroism spectra and the crystal structure of FNR-S96V indicate that this mutant folds properly. FNR-S96V shows only 0.05% of wild-type activity, while the affinities for both ferredoxin and NADP+ are virtually unchanged. However, spectral perturbations induced by NADP+ binding to FNR-S96V strongly resemble those elicited by the binding of 2'-monophosphoadenosine-5'-diphosphoribose, a substrate analog lacking the nicotinamide ring, both to the mutant and wild-type enzymes. Rapid reaction studies on the valine mutant failed to detect charge-transfer intermediates during flavin reduction by NADPH. In addition, no semiquinone formation was seen during photoreduction of FNR-S96V. The three-dimensional structure of the valine mutant shows small, albeit definite, changes only in the isoalloxazine microenvironment. The glycine mutant of FNR displays behavior intermediate between that of wild-type enzyme and that of the valine mutant. It maintains ca. 2% of the wild-type activity as well as the ability to form the charge-transfer species between reduced FNR and NADP+. In photoreduction experiments, the same degree of flavin semiquinone stabilization was observed with FNR-S96G and with the wild-type enzyme. NADP+ binding to the glycine mutant was very similar to that observed in the case of the valine mutant.(ABSTRACT TRUNCATED AT 250 WORDS)
Check<jmol>
 
  <jmolCheckbox>
==About this Structure==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fr/1frn_consurf.spt"</scriptWhenChecked>
1FRN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FRN OCA].  
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==Reference==
  </jmolCheckbox>
Involvement of serine 96 in the catalytic mechanism of ferredoxin-NADP+ reductase: structure--function relationship as studied by site-directed mutagenesis and X-ray crystallography., Aliverti A, Bruns CM, Pandini VE, Karplus PA, Vanoni MA, Curti B, Zanetti G, Biochemistry. 1995 Jul 4;34(26):8371-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7677850 7677850]
</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=1frn ConSurf].
[[Category: Single protein]]
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Spinacia oleracea]]
[[Category: Spinacia oleracea]]
[[Category: Bruns, C M.]]
[[Category: Bruns CM]]
[[Category: Karplus, P A.]]
[[Category: Karplus PA]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:41:13 2008''

Latest revision as of 07:18, 7 February 2024

THE INVOLVEMENT OF SER96 IN THE CATALYTIC MECHANISM OF FERREDOXIN-NADP+ REDUCTASE: STRUCTURE-FUNCTION RELATIONSHIP AS STUDIED BY SITE-DIRECTED MUTAGENESIS AND X-RAY CRYSTALLOGRAPHY

1frn, resolution 2.00Å

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