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Literature summary for extracted from

  • Crain, A.V.; Broderick, J.B.
    Flavodoxin cofactor binding induces structural changes that are required for protein-protein interactions with NADP(+) oxidoreductase and pyruvate formate-lyase activating enzyme (2013), Biochim. Biophys. Acta, 1834, 2512-2519.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
modeling of the complex between pyruvate formate-lyase activating enzyme and flavodoxin. In the pyruvate formate-lyase activating enzyme/flavodoxin complex, FMN is located 10.7 A from the [4Fe-4S] cluster in pyruvate formate-lyase activating enzyme. The flavodoxin binding site on pyruvate formate-lyase activating enzyme is the only location other than the pyruvate formate-lyase binding site where the [4Fe-4S] cluster is close to the surface of the enzyme, which would be necessary for efficient electron transfer Escherichia coli


Organism UniProt Comment Textmining
Escherichia coli


Synonyms Comment Organism
Escherichia coli

General Information

General Information Comment Organism
physiological function holo-flavodoxin is capable of associating with NADP+-dependent flavodoxin oxidoreductase and pyruvate formate-lyase activating enzyme, whereas there is no detectable interaction between apo-flavodoxin. Holo-flavodoxin interacts with pyruvate formate-lyase activating enzyme with a dissociation constant of 23.3 microM Escherichia coli