1qfy: Difference between revisions

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New page: left|200px<br /><applet load="1qfy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qfy, resolution 1.8Å" /> '''PEA FNR Y308S MUTANT ...
 
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[[Image:1qfy.gif|left|200px]]<br /><applet load="1qfy" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1qfy, resolution 1.8&Aring;" />
'''PEA FNR Y308S MUTANT IN COMPLEX WITH NADP+'''<br />


==Overview==
==PEA FNR Y308S MUTANT IN COMPLEX WITH NADP+==
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.
<StructureSection load='1qfy' size='340' side='right'caption='[[1qfy]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1qfy]] 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=1QFY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QFY FirstGlance]. <br>
1QFY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum] with SO4, FAD and NAP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QFY OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</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=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qfy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qfy OCA], [https://pdbe.org/1qfy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qfy RCSB], [https://www.ebi.ac.uk/pdbsum/1qfy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qfy ProSAT]</span></td></tr>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=10467097 10467097]
</table>
[[Category: Ferredoxin--NADP(+) reductase]]
== 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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qf/1qfy_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1qfy ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pisum sativum]]
[[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: FAD]]
[[Category: NAP]]
[[Category: SO4]]
[[Category: electron transfer]]
[[Category: flavoenzyme]]
[[Category: hydride transfer]]
[[Category: photosynthesis]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:39:18 2007''

Latest revision as of 09:11, 3 April 2024

PEA FNR Y308S MUTANT IN COMPLEX WITH NADP+PEA FNR Y308S MUTANT IN COMPLEX WITH NADP+

Structural highlights

1qfy is a 2 chain structure with sequence from Pisum sativum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1qfy, resolution 1.80Å

Drag the structure with the mouse to rotate

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