1qg0

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[[Image:1qg0.gif|left|200px]]
 
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==WILD-TYPE PEA FNR==
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The line below this paragraph, containing "STRUCTURE_1qg0", creates the "Structure Box" on the page.
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<StructureSection load='1qg0' size='340' side='right'caption='[[1qg0]], [[Resolution|resolution]] 2.50&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'>[[1qg0]] 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=1QG0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QG0 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.5&#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></td></tr>
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{{STRUCTURE_1qg0| PDB=1qg0 | 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=1qg0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qg0 OCA], [https://pdbe.org/1qg0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qg0 RCSB], [https://www.ebi.ac.uk/pdbsum/1qg0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qg0 ProSAT]</span></td></tr>
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</table>
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'''WILD-TYPE PEA FNR'''
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== Function ==
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[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.
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== Evolutionary Conservation ==
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==Overview==
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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/qg/1qg0_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=1qg0 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 ==
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.
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.
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==About this Structure==
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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:10467097<ref>PMID:10467097</ref>
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1QG0 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=1QG0 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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]
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</div>
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<div class="pdbe-citations 1qg0" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Pisum sativum]]
[[Category: Pisum sativum]]
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[[Category: Single protein]]
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[[Category: Aliverti A]]
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[[Category: Aliverti, A.]]
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[[Category: Arakaki AK]]
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[[Category: Arakaki, A K.]]
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[[Category: Calcaterra NB]]
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[[Category: Calcaterra, N B.]]
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[[Category: Carrillo N]]
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[[Category: Carrillo, N.]]
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[[Category: Ceccarelli EA]]
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[[Category: Ceccarelli, E A.]]
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[[Category: Deng Z]]
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[[Category: Deng, Z.]]
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[[Category: Karplus PA]]
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[[Category: Karplus, P A.]]
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[[Category: Orellano EG]]
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[[Category: Orellano, E G.]]
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[[Category: Ottado J]]
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[[Category: Ottado, J.]]
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[[Category: Zanetti G]]
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[[Category: Zanetti, G.]]
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[[Category: Electron transfer]]
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[[Category: Flavoenzyme]]
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[[Category: Hydride transfer]]
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[[Category: Photosynthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:13:23 2008''
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Current revision

WILD-TYPE PEA FNR

PDB ID 1qg0

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