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[[Image:1gjr.gif|left|200px]]<br />
<applet load="1gjr" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1gjr, resolution 2.1&Aring;" />
'''FERREDOXIN-NADP+ REDUCTASE COMPLEXED WITH NADP+ BY COCRYSTALLIZATION'''<br />


==Overview==
==Ferredoxin-NADP+ Reductase complexed with NADP+ by COCRYSTALLIZATION==
The flavoenzyme ferredoxin-NADP+ reductase (FNR) catalyses the production, of NADPH in photosynthesis. The three-dimensional structure of FNR, presents two distinct domains, one for binding of the FAD prosthetic group, and the other for NADP+ binding. In spite of extensive experiments and, different crystallographic approaches, many aspects about how the NADP+, substrate binds to FNR and how the hydride ion is transferred from FAD to, NADP+ remain unclear. The structure of an FNR:NADP+ complex from Anabaena, has been determined by X-ray diffraction analysis of the cocrystallised, units to 2.1 A resolution. Structural perturbation of FNR induced by, complex formation produces a narrower cavity in which the 2'-phospho-AMP, and pyrophosphate portions of the NADP+ are perfectly bound. In addition, the nicotinamide mononucleotide moiety is placed in a new pocket created, near the FAD cofactor with the ribose being in a tight conformation. The, crystal structure of this FNR:NADP+ complex obtained by cocrystallisation, displays NADP+ in an unusual conformation and can be considered as an, intermediate state in the process of coenzyme recognition and binding., Structural analysis and comparison with previously reported complexes, allow us to postulate a mechanism which would permit efficient hydride, transfer to occur. Besides, this structure gives new insights into the, postulated formation of the ferredoxin:FNR:NADP+ ternary complex by, prediction of new intermolecular interactions, which could only exist, after FNR:NADP+ complex formation. Finally, structural comparison with the, members of the broad FNR structural family also provides an explanation, for the high specificity exhibited by FNR for NADP+/H versus NAD+/H.
<StructureSection load='1gjr' size='340' side='right'caption='[[1gjr]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1gjr]] is a 1 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=1GJR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GJR FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#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></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gjr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gjr OCA], [https://pdbe.org/1gjr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gjr RCSB], [https://www.ebi.ac.uk/pdbsum/1gjr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gjr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FENR_NOSSO FENR_NOSSO]
== 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/gj/1gjr_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=1gjr ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The flavoenzyme ferredoxin-NADP+ reductase (FNR) catalyses the production of NADPH in photosynthesis. The three-dimensional structure of FNR presents two distinct domains, one for binding of the FAD prosthetic group and the other for NADP+ binding. In spite of extensive experiments and different crystallographic approaches, many aspects about how the NADP+ substrate binds to FNR and how the hydride ion is transferred from FAD to NADP+ remain unclear. The structure of an FNR:NADP+ complex from Anabaena has been determined by X-ray diffraction analysis of the cocrystallised units to 2.1 A resolution. Structural perturbation of FNR induced by complex formation produces a narrower cavity in which the 2'-phospho-AMP and pyrophosphate portions of the NADP+ are perfectly bound. In addition, the nicotinamide mononucleotide moiety is placed in a new pocket created near the FAD cofactor with the ribose being in a tight conformation. The crystal structure of this FNR:NADP+ complex obtained by cocrystallisation displays NADP+ in an unusual conformation and can be considered as an intermediate state in the process of coenzyme recognition and binding. Structural analysis and comparison with previously reported complexes allow us to postulate a mechanism which would permit efficient hydride transfer to occur. Besides, this structure gives new insights into the postulated formation of the ferredoxin:FNR:NADP+ ternary complex by prediction of new intermolecular interactions, which could only exist after FNR:NADP+ complex formation. Finally, structural comparison with the members of the broad FNR structural family also provides an explanation for the high specificity exhibited by FNR for NADP+/H versus NAD+/H.


==About this Structure==
Mechanism of coenzyme recognition and binding revealed by crystal structure analysis of ferredoxin-NADP+ reductase complexed with NADP+.,Hermoso JA, Mayoral T, Faro M, Gomez-Moreno C, Sanz-Aparicio J, Medina M J Mol Biol. 2002 Jun 21;319(5):1133-42. PMID:12079352<ref>PMID:12079352</ref>
1GJR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.] with 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] Structure known Active Site: FAD. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GJR OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Mechanism of coenzyme recognition and binding revealed by crystal structure analysis of ferredoxin-NADP+ reductase complexed with NADP+., Hermoso JA, Mayoral T, Faro M, Gomez-Moreno C, Sanz-Aparicio J, Medina M, J Mol Biol. 2002 Jun 21;319(5):1133-42. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12079352 12079352]
</div>
[[Category: Anabaena sp.]]
<div class="pdbe-citations 1gjr" style="background-color:#fffaf0;"></div>
[[Category: Ferredoxin--NADP(+) reductase]]
== References ==
[[Category: Single protein]]
<references/>
[[Category: Gomez-Moreno, C.]]
__TOC__
[[Category: Hermoso, J.A.]]
</StructureSection>
[[Category: Mayoral, T.]]
[[Category: Large Structures]]
[[Category: Medina, M.]]
[[Category: Nostoc sp. PCC 7119]]
[[Category: Sanz-Aparicio, J.]]
[[Category: Gomez-Moreno C]]
[[Category: FAD]]
[[Category: Hermoso JA]]
[[Category: NAP]]
[[Category: Mayoral T]]
[[Category: fad]]
[[Category: Medina M]]
[[Category: flavoprotein]]
[[Category: Sanz-Aparicio J]]
[[Category: fnr]]
[[Category: nadp]]
[[Category: nadp reductase]]
[[Category: oxidoreductase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov  5 16:13:48 2007''

Latest revision as of 14:58, 13 December 2023

Ferredoxin-NADP+ Reductase complexed with NADP+ by COCRYSTALLIZATIONFerredoxin-NADP+ Reductase complexed with NADP+ by COCRYSTALLIZATION

Structural highlights

1gjr is a 1 chain structure with sequence from Nostoc sp. PCC 7119. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FENR_NOSSO

Evolutionary Conservation

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

Publication Abstract from PubMed

The flavoenzyme ferredoxin-NADP+ reductase (FNR) catalyses the production of NADPH in photosynthesis. The three-dimensional structure of FNR presents two distinct domains, one for binding of the FAD prosthetic group and the other for NADP+ binding. In spite of extensive experiments and different crystallographic approaches, many aspects about how the NADP+ substrate binds to FNR and how the hydride ion is transferred from FAD to NADP+ remain unclear. The structure of an FNR:NADP+ complex from Anabaena has been determined by X-ray diffraction analysis of the cocrystallised units to 2.1 A resolution. Structural perturbation of FNR induced by complex formation produces a narrower cavity in which the 2'-phospho-AMP and pyrophosphate portions of the NADP+ are perfectly bound. In addition, the nicotinamide mononucleotide moiety is placed in a new pocket created near the FAD cofactor with the ribose being in a tight conformation. The crystal structure of this FNR:NADP+ complex obtained by cocrystallisation displays NADP+ in an unusual conformation and can be considered as an intermediate state in the process of coenzyme recognition and binding. Structural analysis and comparison with previously reported complexes allow us to postulate a mechanism which would permit efficient hydride transfer to occur. Besides, this structure gives new insights into the postulated formation of the ferredoxin:FNR:NADP+ ternary complex by prediction of new intermolecular interactions, which could only exist after FNR:NADP+ complex formation. Finally, structural comparison with the members of the broad FNR structural family also provides an explanation for the high specificity exhibited by FNR for NADP+/H versus NAD+/H.

Mechanism of coenzyme recognition and binding revealed by crystal structure analysis of ferredoxin-NADP+ reductase complexed with NADP+.,Hermoso JA, Mayoral T, Faro M, Gomez-Moreno C, Sanz-Aparicio J, Medina M J Mol Biol. 2002 Jun 21;319(5):1133-42. PMID:12079352[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Hermoso JA, Mayoral T, Faro M, Gomez-Moreno C, Sanz-Aparicio J, Medina M. Mechanism of coenzyme recognition and binding revealed by crystal structure analysis of ferredoxin-NADP+ reductase complexed with NADP+. J Mol Biol. 2002 Jun 21;319(5):1133-42. PMID:12079352 doi:10.1016/S0022-2836(02)00388-1

1gjr, resolution 2.10Å

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