Pyruvate-ferredoxin oxidoreductase

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<Structure load='2c3o' size='400' frame='true' align='right' caption=' Pyruvate-ferredoxin oxidoredoxin with Fe4S4 cluster complex with thiamin diphosphate and pyruvate [[2c3o]]' scene= />
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<StructureSection load='2c3o' size='350' side='right' scene='49/490113/Cv/1' caption='Pyruvate-ferredoxin oxidoredoxin dimer with Fe4S4 cluster complex with thiamine diphosphate and pyruvate [[2c3o]]'>
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== Function ==
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Please use the "3D" button above this box to insert a Jmol applet (molecule) on this page.
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'''Pyruvate-ferredoxin oxidoreductase''' (PFOR) is an enzyme of the fermentation cycle which catalyzes the oxidative decarboxylation of pyruvate to acetyl CoA and CO<sub>2</sub>. This reaction provides the electron source for the reduction of ferredoxin<ref>PMID:10878009</ref>. The reaction is CoA-dependent and contains thiamine diphosphate (TDP). PFOR contains iron-sulfur clusters (Fe<sub>4</sub>S<sub>4</sub>).
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Or use the four-green-boxes-button to insert scrollable text adjacent
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to a Jmol applet. Check out the other buttons as well!
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'''Pyruvate-ferredoxin oxidoreductase''' (PFOR) is an enzyme of the fermentation cycle which catalyzes the oxidative decarboxylation of pyruvate to acetyl CoA and CO2. This reaction provides the electron source for the reduction of ferredoxin. The reaction is CoA-dependent and contains thiamine diphosphate (TDP). PFOR contains iron-sulfur clusters (Fe4S4).
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== Structural highlights ==
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The <scene name='49/490113/Cv/6'>active site of PFOR contains thiamine diphosphate and pyruvate</scene><ref>PMID:16472741</ref>. <scene name='49/490113/Cv/7'>Mg coordination site</scene>. Water molecules are shown as red spheres. <scene name='49/490113/Cv/8'>Fe4S4 cluster interactions</scene>. Each Fe atom interacts with S atom from cysteine.
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</StructureSection>
==3D structures of pyruvate-ferredoxin oxidoreductase==
==3D structures of pyruvate-ferredoxin oxidoreductase==
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{{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
[[1b0p]], [[2c3m]] – DaPFOR + TDP – ''Desulfovibrio africanus''<br />
[[1b0p]], [[2c3m]] – DaPFOR + TDP – ''Desulfovibrio africanus''<br />
[[2pda]], [[2c3o]], [[2c42]] - DaPFOR + pyruvate + TDP<br />
[[2pda]], [[2c3o]], [[2c42]] - DaPFOR + pyruvate + TDP<br />
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[[1kek]], [[2c3y]] - DaPFOR + CO2 + acetyl-TDP<br />
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[[1kek]], [[2c3y]], [[2uza]] - DaPFOR + CO2 + acetyl-TDP<br />
[[2c3p]] - DaPFOR + TDP derivative<br />
[[2c3p]] - DaPFOR + TDP derivative<br />
[[2c3u]] - DaPFOR + pyruvate + TDP derivative<br />
[[2c3u]] - DaPFOR + pyruvate + TDP derivative<br />
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[[2raa]] - PFOR γ subunit - ''Thermotoga maritima''
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[[7plm]] – DaPFOR + TPP – Cryo EM<br />
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[[2raa]] - PFOR γ subunit - ''Thermotoga maritima''<br />
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[[6cin]] – MtPFOR + TDP – ''Moorella thermoacetica''<br />
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[[6cio]], [[6cip]] – MtPFOR + TTP derivative <br />
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[[6ciq]] – MtPFOR + TTP + CoA <br />
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Pyruvate-ferredoxin oxidoredoxin dimer with Fe4S4 cluster complex with thiamine diphosphate and pyruvate 2c3o

Drag the structure with the mouse to rotate

3D structures of pyruvate-ferredoxin oxidoreductase

04-October-2023

1b0p, 2c3m – DaPFOR + TDP – Desulfovibrio africanus
2pda, 2c3o, 2c42 - DaPFOR + pyruvate + TDP
1kek, 2c3y, 2uza - DaPFOR + CO2 + acetyl-TDP
2c3p - DaPFOR + TDP derivative
2c3u - DaPFOR + pyruvate + TDP derivative
7plm – DaPFOR + TPP – Cryo EM
2raa - PFOR γ subunit - Thermotoga maritima
6cin – MtPFOR + TDP – Moorella thermoacetica
6cio, 6cip – MtPFOR + TTP derivative
6ciq – MtPFOR + TTP + CoA


References

  1. ↑ Furdui C, Ragsdale SW. The role of pyruvate ferredoxin oxidoreductase in pyruvate synthesis during autotrophic growth by the Wood-Ljungdahl pathway. J Biol Chem. 2000 Sep 15;275(37):28494-9. PMID:10878009 doi:http://dx.doi.org/10.1074/jbc.M003291200
  2. ↑ Cavazza C, Contreras-Martel C, Pieulle L, Chabriere E, Hatchikian EC, Fontecilla-Camps JC. Flexibility of thiamine diphosphate revealed by kinetic crystallographic studies of the reaction of pyruvate-ferredoxin oxidoreductase with pyruvate. Structure. 2006 Feb;14(2):217-24. PMID:16472741 doi:10.1016/j.str.2005.10.013

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Michal Harel, Alexander Berchansky

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