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| <StructureSection load='5vj7' size='340' side='right'caption='[[5vj7]], [[Resolution|resolution]] 2.55Å' scene=''> | | <StructureSection load='5vj7' size='340' side='right'caption='[[5vj7]], [[Resolution|resolution]] 2.55Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[5vj7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus_com1 Pyrococcus furiosus com1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VJ7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VJ7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5vj7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus_COM1 Pyrococcus furiosus COM1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VJ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VJ7 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=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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]] 2.55Å</td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PFC_09035 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1185654 Pyrococcus furiosus COM1]), PFC_09030 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1185654 Pyrococcus furiosus COM1])</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=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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=5vj7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vj7 OCA], [https://pdbe.org/5vj7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vj7 RCSB], [https://www.ebi.ac.uk/pdbsum/5vj7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vj7 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=5vj7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vj7 OCA], [http://pdbe.org/5vj7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vj7 RCSB], [http://www.ebi.ac.uk/pdbsum/5vj7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vj7 ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/I6V148_9EURY I6V148_9EURY] |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Pyrococcus furiosus com1]] | + | [[Category: Pyrococcus furiosus COM1]] |
- | [[Category: Adams, M W.W]] | + | [[Category: Adams MWW]] |
- | [[Category: Lipscomb, G L]] | + | [[Category: Lipscomb GL]] |
- | [[Category: Nguyen, D M.N]] | + | [[Category: Nguyen DMN]] |
- | [[Category: Peters, J W]] | + | [[Category: Peters JW]] |
- | [[Category: Schut, G J]] | + | [[Category: Schut GJ]] |
- | [[Category: Tokmina-Lukaszewska, M]] | + | [[Category: Tokmina-Lukaszewska M]] |
- | [[Category: Zadvornyy, O A]] | + | [[Category: Zadvornyy OA]] |
- | [[Category: Archaea]]
| + | |
- | [[Category: Electron bifurcation]]
| + | |
- | [[Category: Hyperthermophile]]
| + | |
- | [[Category: Metabolism]]
| + | |
- | [[Category: Nfnii]]
| + | |
- | [[Category: Oxidoreductase]]
| + | |
- | [[Category: Sulfur]]
| + | |
| Structural highlights
Function
I6V148_9EURY
Publication Abstract from PubMed
Electron bifurcation has recently gained acceptance as the third mechanism of energy conservation in which energy is conserved through the coupling of exergonic and endergonic reactions. A structure-based mechanism of bifurcation has been elucidated recently for the flavin-based enzyme NADH-dependent ferredoxin NADP+ oxidoreductase I (NfnI) from the hyperthermophillic archaeon Pyrococcus furiosus. NfnI is thought to be involved in maintaining the cellular redox balance, producing NADPH for biosynthesis by recycling the two other primary redox carriers, NADH and ferredoxin. The P. furiosus genome encodes an NfnI paralog termed NfnII, and the two are differentially expressed, depending on the growth conditions. In this study, we show that deletion of the genes encoding either NfnI or NfnII affects the cellular concentrations of NAD(P)H and particularly NADPH. This results in a moderate to severe growth phenotype in deletion mutants, demonstrating a key role for each enzyme in maintaining redox homeostasis. Despite their similarity in primary sequence and cofactor content, crystallographic, kinetic, and mass spectrometry analyses reveal that there are fundamental structural differences between the two enzymes, and NfnII does not catalyze the NfnI bifurcating reaction. Instead, it exhibits non-bifurcating ferredoxin NADP oxidoreductase-type activity. NfnII is therefore proposed to be a bifunctional enzyme and also to catalyze a bifurcating reaction, although its third substrate, in addition to ferredoxin and NADP(H), is as yet unknown.
Two functionally distinct NADP+-dependent ferredoxin oxidoreductases maintain the primary redox balance of Pyrococcus furiosus.,Nguyen DMN, Schut GJ, Zadvornyy OA, Tokmina-Lukaszewska M, Poudel S, Lipscomb GL, Adams LA, Dinsmore JT, Nixon WJ, Boyd ES, Bothner B, Peters JW, Adams MWW J Biol Chem. 2017 Sep 1;292(35):14603-14616. doi: 10.1074/jbc.M117.794172. Epub, 2017 Jul 13. PMID:28705933[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nguyen DMN, Schut GJ, Zadvornyy OA, Tokmina-Lukaszewska M, Poudel S, Lipscomb GL, Adams LA, Dinsmore JT, Nixon WJ, Boyd ES, Bothner B, Peters JW, Adams MWW. Two functionally distinct NADP+-dependent ferredoxin oxidoreductases maintain the primary redox balance of Pyrococcus furiosus. J Biol Chem. 2017 Sep 1;292(35):14603-14616. doi: 10.1074/jbc.M117.794172. Epub, 2017 Jul 13. PMID:28705933 doi:http://dx.doi.org/10.1074/jbc.M117.794172
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