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| | ==FERREDOXIN-NADP+ REDUCTASE (MUTATION: E 301 A)== | | ==FERREDOXIN-NADP+ REDUCTASE (MUTATION: E 301 A)== |
| - | <StructureSection load='1b2r' size='340' side='right' caption='[[1b2r]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='1b2r' size='340' side='right'caption='[[1b2r]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1b2r]] 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=1B2R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1B2R FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1b2r]] 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=1B2R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B2R 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=SO4:SULFATE+ION'>SO4</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]] 1.8Å</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='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=SO4:SULFATE+ION'>SO4</scene></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=1b2r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b2r OCA], [http://pdbe.org/1b2r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1b2r RCSB], [http://www.ebi.ac.uk/pdbsum/1b2r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1b2r ProSAT]</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=1b2r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b2r OCA], [https://pdbe.org/1b2r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b2r RCSB], [https://www.ebi.ac.uk/pdbsum/1b2r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b2r 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: Gomez-Moreno, C]] | + | [[Category: Nostoc sp. PCC 7119]] |
| - | [[Category: Hermoso, J A]] | + | [[Category: Gomez-Moreno C]] |
| - | [[Category: Martinez-Julvez, M]] | + | [[Category: Hermoso JA]] |
| - | [[Category: Martinez-Ripoll, M]] | + | [[Category: Martinez-Julvez M]] |
| - | [[Category: Mayoral, T]] | + | [[Category: Martinez-Ripoll M]] |
| - | [[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 three-dimensional crystal structure of the Glu301Ala site-directed mutant of ferredoxin-NADP+ reductase from Anabaena PCC 7119 has been determined at 1.8A resolution by x-ray diffraction. The overall folding of the Glu301Ala FNR mutant shows no significant differences with respect to that of the wild-type enzyme. However, interesting conformational changes are detected in the side chain of another glutamate residue, Glu139, which now points towards the FAD cofactor in the active center cavity. The new conformation of the Glu139 side chain is stabilized by a network of five hydrogen bonds to several water molecules, which seem to hold the carboxylate side chain in a rather fixed position. This interacting network connects the Glu139 side chain to the Ser80 side chain through a series of three water molecules. These observations are discussed in terms of the reactivity of Glu301Ala ferredoxin-NADP+ reductase towards its substrates, and the role of Glu301 in the catalysis is re-examined. Moreover, a structural explanation of the different reoxidation properties of this mutant is given on the basis of the reported structure by modeling the hypothetical flavin C(4a)-hydroperoxide intermediate. The model shows that the distal oxygen of the peroxide anion could be in an appropriate situation to act as the proton donor in the reoxidation process.
Structural basis of the catalytic role of Glu301 in Anabaena PCC 7119 ferredoxin-NADP+ reductase revealed by x-ray crystallography.,Mayoral T, Medina M, Sanz-Aparicio J, Gomez-Moreno C, Hermoso JA Proteins. 2000 Jan 1;38(1):60-9. PMID:10651039[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mayoral T, Medina M, Sanz-Aparicio J, Gomez-Moreno C, Hermoso JA. Structural basis of the catalytic role of Glu301 in Anabaena PCC 7119 ferredoxin-NADP+ reductase revealed by x-ray crystallography. Proteins. 2000 Jan 1;38(1):60-9. PMID:10651039
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