Pyruvate-ferredoxin oxidoreductase
From Proteopedia
(Difference between revisions)
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| - | < | + | <StructureSection load='2c3o' size='400' side='right' scene='' caption='Pyruvate-ferredoxin oxidoredoxin dimer with Fe4S4 cluster complex with thiamin diphosphate and pyruvate [[2c3o]]'> |
== Function == | == Function == | ||
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== Structural highlights == | == Structural highlights == | ||
The active site of PFOR contains thiamine diphosphate and pyruvate<ref>PMID:16472741</ref>. | The active site of PFOR contains thiamine diphosphate and pyruvate<ref>PMID:16472741</ref>. | ||
| - | + | </StructureSection> | |
==3D structures of pyruvate-ferredoxin oxidoreductase== | ==3D structures of pyruvate-ferredoxin oxidoreductase== | ||
Revision as of 09:53, 2 August 2016
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3D structures of pyruvate-ferredoxin oxidoreductase
Update June 2012
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
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
