Pyruvate-ferredoxin oxidoreductase
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
| - | The <scene name='49/490113/Cv/6'>active site of PFOR contains thiamine diphosphate and pyruvate</scene><ref>PMID:16472741</ref>. Water molecules are shown as red spheres. <scene name='49/490113/Cv/ | + | 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>. |
</StructureSection> | </StructureSection> | ||
==3D structures of pyruvate-ferredoxin oxidoreductase== | ==3D structures of pyruvate-ferredoxin oxidoreductase== | ||
Revision as of 13:11, 22 August 2019
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3D structures of pyruvate-ferredoxin oxidoreductase
22-August-2019
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
2raa - PFOR γ subunit - Thermotoga maritima
6cin – MtPFOR + TDP – Moorella thermoacetica
6cio, 6cip – MtPFOR + TTP derivative
6ciq – MtPFOR + TTP + CoA
References
- ↑ 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
- ↑ 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
