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==NADH-dependent Ferredoxin:NADP Oxidoreductase (NfnI) from Pyrococcus furiosus==
==NADH-dependent Ferredoxin:NADP Oxidoreductase (NfnI) from Pyrococcus furiosus==
<StructureSection load='5jfc' size='340' side='right' caption='[[5jfc]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='5jfc' size='340' side='right'caption='[[5jfc]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5jfc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JFC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JFC FirstGlance]. <br>
<table><tr><td colspan='2'>[[5jfc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JFC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JFC 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]] 1.598&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5jca|5jca]]</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/NAD(P)(+)_transhydrogenase_(ferredoxin) NAD(P)(+) transhydrogenase (ferredoxin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.1.4 1.6.1.4] </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=5jfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jfc OCA], [https://pdbe.org/5jfc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jfc RCSB], [https://www.ebi.ac.uk/pdbsum/5jfc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jfc 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=5jfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jfc OCA], [http://pdbe.org/5jfc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jfc RCSB], [http://www.ebi.ac.uk/pdbsum/5jfc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jfc ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/SUDHA_PYRFU SUDHA_PYRFU]] A bifunctional enzyme that catalyzes the reduction of elemental sulfur or polysulfide to hydrogen sulfide with NADPH as electron donor. Also functions as a reduced ferredoxin:NADP oxidoreductase with a very high affinity for reduced ferredoxin. Exhibits a broad specificity for various physiological and non-physiological substrates with varied reduction potentials such as methyl viologen, benzyl viologen, FAD, FMN, methylene blue, 2,6-dichlorophenolindophenol (DCIP), cytochrome C and ferricyanide with highest preference for benzyl viologen. Does not reduce fumarate, succinate, nitrate, nitrite, sulfate, sulfite or protons. Does not possess any hydrogenase activity or NADPH-dependent glutamate synthase activity.<ref>PMID:10968624</ref> <ref>PMID:7961401</ref> [REFERENCE:4] [[http://www.uniprot.org/uniprot/SUDHB_PYRFU SUDHB_PYRFU]] A bifunctional enzyme that catalyzes the reduction of elemental sulfur or polysulfide to hydrogen sulfide with NADPH as electron donor. Also functions as a reduced ferredoxin:NADP oxidoreductase with a very high affinity for reduced ferredoxin. Exhibits a broad specificity for various physiological and non-physiological substrates with varied reduction potentials such as methyl viologen, benzyl viologen, FAD, FMN, methylene blue, 2,6-dichlorophenolindophenol (DCIP), cytochrome C and ferricyanide with highest preference for benzyl viologen. Does not reduce fumarate, succinate, nitrate, nitrite, sulfate, sulfite or protons. Does not possess any hydrogenase activity or NADPH-dependent glutamate synthase activity.<ref>PMID:10968624</ref> <ref>PMID:7961401</ref> <ref>PMID:7961401</ref> 
[https://www.uniprot.org/uniprot/SUDHA_PYRFU SUDHA_PYRFU] A bifunctional enzyme that catalyzes the reduction of elemental sulfur or polysulfide to hydrogen sulfide with NADPH as electron donor. Also functions as a reduced ferredoxin:NADP oxidoreductase with a very high affinity for reduced ferredoxin. Exhibits a broad specificity for various physiological and non-physiological substrates with varied reduction potentials such as methyl viologen, benzyl viologen, FAD, FMN, methylene blue, 2,6-dichlorophenolindophenol (DCIP), cytochrome C and ferricyanide with highest preference for benzyl viologen. Does not reduce fumarate, succinate, nitrate, nitrite, sulfate, sulfite or protons. Does not possess any hydrogenase activity or NADPH-dependent glutamate synthase activity.<ref>PMID:10968624</ref> <ref>PMID:7961401</ref> [REFERENCE:4]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Pyrococcus furiosus]]
[[Category: Pyrococcus furiosus]]
[[Category: Adams, M W]]
[[Category: Adams MW]]
[[Category: Artz, J H]]
[[Category: Artz JH]]
[[Category: King, P W]]
[[Category: King PW]]
[[Category: Lipscomb, G]]
[[Category: Lipscomb G]]
[[Category: Nguyen, D M]]
[[Category: Nguyen DM]]
[[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: Nfni]]
[[Category: Oxidoreductase]]

Latest revision as of 15:37, 6 March 2024

NADH-dependent Ferredoxin:NADP Oxidoreductase (NfnI) from Pyrococcus furiosusNADH-dependent Ferredoxin:NADP Oxidoreductase (NfnI) from Pyrococcus furiosus

Structural highlights

5jfc is a 2 chain structure with sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.598Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SUDHA_PYRFU A bifunctional enzyme that catalyzes the reduction of elemental sulfur or polysulfide to hydrogen sulfide with NADPH as electron donor. Also functions as a reduced ferredoxin:NADP oxidoreductase with a very high affinity for reduced ferredoxin. Exhibits a broad specificity for various physiological and non-physiological substrates with varied reduction potentials such as methyl viologen, benzyl viologen, FAD, FMN, methylene blue, 2,6-dichlorophenolindophenol (DCIP), cytochrome C and ferricyanide with highest preference for benzyl viologen. Does not reduce fumarate, succinate, nitrate, nitrite, sulfate, sulfite or protons. Does not possess any hydrogenase activity or NADPH-dependent glutamate synthase activity.[1] [2] [REFERENCE:4]

References

  1. ↑ Hagen WR, Silva PJ, Amorim MA, Hagedoorn PL, Wassink H, Haaker H, Robb FT. Novel structure and redox chemistry of the prosthetic groups of the iron-sulfur flavoprotein sulfide dehydrogenase from Pyrococcus furiosus; evidence for a [2Fe-2S] cluster with Asp(Cys)3 ligands. J Biol Inorg Chem. 2000 Aug;5(4):527-34. PMID:10968624
  2. ↑ Ma K, Adams MW. Sulfide dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus: a new multifunctional enzyme involved in the reduction of elemental sulfur. J Bacteriol. 1994 Nov;176(21):6509-17. PMID:7961401

5jfc, resolution 1.60Å

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