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| | <StructureSection load='1gjr' size='340' side='right'caption='[[1gjr]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='1gjr' size='340' side='right'caption='[[1gjr]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1gjr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Anabaena_pcc7119 Anabaena pcc7119]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GJR FirstGlance]. <br> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b2r|1b2r]], [[1bjk|1bjk]], [[1e62|1e62]], [[1e63|1e63]], [[1e64|1e64]], [[1ewy|1ewy]], [[1h85|1h85]], [[1que|1que]], [[1quf|1quf]]</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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='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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gjr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gjr OCA], [http://pdbe.org/1gjr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gjr RCSB], [http://www.ebi.ac.uk/pdbsum/1gjr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gjr ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/FENR_NOSSO FENR_NOSSO] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Anabaena pcc7119]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Gomez-Moreno, C]] | + | [[Category: Nostoc sp. PCC 7119]] |
| - | [[Category: Hermoso, J A]] | + | [[Category: Gomez-Moreno C]] |
| - | [[Category: Mayoral, T]] | + | [[Category: Hermoso JA]] |
| - | [[Category: Medina, M]] | + | [[Category: Mayoral T]] |
| - | [[Category: Sanz-Aparicio, J]] | + | [[Category: Medina M]] |
| - | [[Category: Fad]]
| + | [[Category: Sanz-Aparicio J]] |
| - | [[Category: Flavoprotein]]
| + | |
| - | [[Category: Fnr]]
| + | |
| - | [[Category: Nadp]]
| + | |
| - | [[Category: Nadp reductase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
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
- ↑ 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
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