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EC Number
apo-enzyme, to 1.85 A resolution. Apo-LuxF possesses four preorganized binding sites for 6-(3'-(R)-myristyl)-FMN
bacterial luciferase/FMN complex, by the hanging drop method, at 2.3 A resolution. Crystals of recombinant luciferase are grown at room temperature prior to soaking with millimolar concentrations of FMN. Belongs to space group P212121. The isoalloxazine ring is coordinated by an unusual cis-Ala-Ala peptide bond. The reactive sulfhydryl group of Cys106 projects toward position C-4a, the site of flavin oxygenation. Mobile loop that is crystallographically disordered, appears to be a boundary between solvent and the active center. Within this portion of the protein, there is a single contact between Phe272 of the R subunit and Tyr151 of the beta subunit
structure is determined in absence of substrate at low-salt concentrations
Results 1 - 4 of 4