1gjr

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[[Image:1gjr.jpg|left|200px]]<br /><applet load="1gjr" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1gjr.jpg|left|200px]]
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caption="1gjr, resolution 2.1&Aring;" />
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'''FERREDOXIN-NADP+ REDUCTASE COMPLEXED WITH NADP+ BY COCRYSTALLIZATION'''<br />
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{{Structure
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|PDB= 1gjr |SIZE=350|CAPTION= <scene name='initialview01'>1gjr</scene>, resolution 2.1&Aring;
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|SITE= <scene name='pdbsite=FAD:Nap+Binding+Site+For+Chain+A'>FAD</scene>
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|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> and <scene name='pdbligand=NAP:NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'>NAP</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''FERREDOXIN-NADP+ REDUCTASE COMPLEXED WITH NADP+ BY COCRYSTALLIZATION'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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 <scene name='pdbligand=FAD:'>FAD</scene> and <scene name='pdbligand=NAP:'>NAP</scene> 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] Known structural/functional Site: <scene name='pdbsite=FAD:Nap+Binding+Site+For+Chain+A'>FAD</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GJR OCA].
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1GJR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GJR OCA].
==Reference==
==Reference==
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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]
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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://www.ncbi.nlm.nih.gov/pubmed/12079352 12079352]
[[Category: Anabaena sp.]]
[[Category: Anabaena sp.]]
[[Category: Ferredoxin--NADP(+) reductase]]
[[Category: Ferredoxin--NADP(+) reductase]]
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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:50:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:24:05 2008''

Revision as of 09:24, 20 March 2008

Image:1gjr.jpg


PDB ID 1gjr

Drag the structure with the mouse to rotate
, resolution 2.1Å
Sites:
Ligands: and
Activity: Ferredoxin--NADP(+) reductase, with EC number 1.18.1.2
Coordinates: save as pdb, mmCIF, xml



FERREDOXIN-NADP+ REDUCTASE COMPLEXED WITH NADP+ BY COCRYSTALLIZATION


Overview

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

1GJR is a Single protein structure of sequence from Anabaena sp.. Full crystallographic information is available from OCA.

Reference

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

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