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Literature summary for 1.97.1.4 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

Organism UniProt Comment Textmining
Escherichia coli
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-
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Synonyms

Synonyms Comment Organism
PFL-AE
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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