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1qfz

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PEA FNR Y308S MUTANT IN COMPLEX WITH NADPH

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Retrieved from "http://52.214.119.220/wiki/index.php/1qfz"

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-[[Image:1qfz.gif|left|200px]]
- {{Structure
+==PEA FNR Y308S MUTANT IN COMPLEX WITH NADPH==
-|PDB= 1qfz |SIZE=350|CAPTION= <scene name='initialview01'>1qfz</scene>, resolution 1.7&Aring;
+<StructureSection load='1qfz' size='340' side='right'caption='[[1qfz]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
+<table><tr><td colspan='2'>[[1qfz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QFZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QFZ FirstGlance]. <br>
-|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferredoxin--NADP(+)_reductase Ferredoxin--NADP(+) reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.1.2 1.18.1.2] </span>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
-|GENE=
+<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=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-|DOMAIN=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qfz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qfz OCA], [https://pdbe.org/1qfz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qfz RCSB], [https://www.ebi.ac.uk/pdbsum/1qfz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qfz ProSAT]</span></td></tr>
-|RELATEDENTRY=
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qfz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qfz OCA], [http://www.ebi.ac.uk/pdbsum/1qfz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qfz RCSB]</span>
+== Function ==
-}}
+[https://www.uniprot.org/uniprot/FENR1_PEA FENR1_PEA] 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 ==
-'''PEA FNR Y308S MUTANT IN COMPLEX WITH NADPH'''
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
-==Overview==
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qf/1qfz_consurf.spt"</scriptWhenChecked>
-The flavoenzyme ferredoxin-NADP+ reductase (FNR) catalyzes the production of NADPH during photosynthesis. Whereas the structures of FNRs from spinach leaf and a cyanobacterium as well as many of their homologs have been solved, none of these studies has yielded a productive geometry of the flavin-nicotinamide interaction. Here, we show that this failure occurs because nicotinamide binding to wild type FNR involves the energetically unfavorable displacement of the C-terminal Tyr side chain. We used mutants of this residue (Tyr 308) of pea FNR to obtain the structures of productive NADP+ and NADPH complexes. These structures reveal a unique NADP+ binding mode in which the nicotinamide ring is not parallel to the flavin isoalloxazine ring, but lies against it at an angle of approximately 30 degrees, with the C4 atom 3 A from the flavin N5 atom.
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
-==About this Structure==
+  </jmolCheckbox>
-QFZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QFZ OCA].
+</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=1qfz ConSurf].
+<div style="clear:both"></div>
-==Reference==
+__TOC__
-A productive NADP+ binding mode of ferredoxin-NADP + reductase revealed by protein engineering and crystallographic studies., Deng Z, Aliverti A, Zanetti G, Arakaki AK, Ottado J, Orellano EG, Calcaterra NB, Ceccarelli EA, Carrillo N, Karplus PA, Nat Struct Biol. 1999 Sep;6(9):847-53. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10467097 10467097]
+</StructureSection>
-[[Category: Ferredoxin--NADP(+) reductase]]
+[[Category: Large Structures]]
 [[Category: Pisum sativum]]
-[[Category: Single protein]]
+[[Category: Aliverti A]]
-[[Category: Aliverti, A.]]
+[[Category: Arakaki AK]]
-[[Category: Arakaki, A K.]]
+[[Category: Calcaterra NB]]
-[[Category: Calcaterra, N B.]]
+[[Category: Carrillo N]]
-[[Category: Carrillo, N.]]
+[[Category: Ceccarelli EA]]
-[[Category: Ceccarelli, E A.]]
+[[Category: Deng Z]]
-[[Category: Deng, Z.]]
+[[Category: Karplus PA]]
-[[Category: Karplus, P A.]]
+[[Category: Orellano EG]]
-[[Category: Orellano, E G.]]
+[[Category: Ottado J]]
-[[Category: Ottado, J.]]
+[[Category: Zanetti G]]
-[[Category: Zanetti, G.]]
-[[Category: electron transfer]]
-[[Category: flavoenzyme]]
-[[Category: hydride transfer]]
-[[Category: photosynthesis]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:12:58 2008''

1qfz

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PEA FNR Y308S MUTANT IN COMPLEX WITH NADPH

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Evolutionary Conservation

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