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2c42
From Proteopedia
| 2c42, resolution 1.78Å () | |||||||||
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| Ligands: | , , , , | ||||||||
| Activity: | Pyruvate synthase, with EC number 1.2.7.1 | ||||||||
| Related: | 1b0p, 1kek, 2pda, 2c3m, 2c3o, 2c3p, 2c3u, 2c3y | ||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Contents |
Crystal Structure Of Pyruvate-Ferredoxin Oxidoreductase From Desulfovibrio africanus
Pyruvate-ferredoxin oxidoreductases (PFOR) are unique among thiamine pyrophosphate (ThDP)-containing enzymes in giving rise to a rather stable cofactor-based free-radical species upon the decarboxylation of their first substrate, pyruvate. We have obtained snapshots of unreacted and partially reacted (probably as a tetrahedral intermediate) pyruvate-PFOR complexes at different time intervals. We conclude that pyruvate decarboxylation involves very limited substrate-to-product movements but a significant displacement of the thiazolium moiety of ThDP. In this respect, PFOR seems to differ substantially from other ThDP-containing enzymes, such as transketolase and pyruvate decarboxylase. In addition, exposure of PFOR to oxygen in the presence of pyruvate results in significant inhibition of catalytic activity, both in solution and in the crystals. Examination of the crystal structure of inhibited PFOR suggests that the loss of activity results from oxime formation at the 4' amino substituent of the pyrimidine moiety of ThDP.
Flexibility of thiamine diphosphate revealed by kinetic crystallographic studies of the reaction of pyruvate-ferredoxin oxidoreductase with pyruvate., Cavazza C, Contreras-Martel C, Pieulle L, Chabriere E, Hatchikian EC, Fontecilla-Camps JC, Structure. 2006 Feb;14(2):217-24. PMID:16472741
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
2c42 is a 2 chain structure with sequence from Desulfovibrio africanus. Full crystallographic information is available from OCA.
See Also
Reference
- 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
- Chabriere E, Vernede X, Guigliarelli B, Charon MH, Hatchikian EC, Fontecilla-Camps JC. Crystal structure of the free radical intermediate of pyruvate:ferredoxin oxidoreductase. Science. 2001 Dec 21;294(5551):2559-63. PMID:11752578 doi:10.1126/science.1066198
Categories: Desulfovibrio africanus | Pyruvate synthase | Cavazza, C. | Chabriere, E. | Contreras-Martel, C. | Fontecilla-Camps, J C. | Hatchikian, E C. | Pieulle, L. | Electron transport | Iron | Iron-sulfur | Iron-sulfur cluster | Metal-binding | Oxidoreductase | Pyruvate catabolism | Tpp-dependent enzyme
