EC Number   |
|---|
   1.1.98.2 | recombinant wild-type and selenomethionine-labeled FGD1, sitting drop vapour diffusion, mixing of protein solution in a 1:1 ratio with precipitant solution containing 1.6 M tri-sodium citrate, pH 6.5, microseeding, X-ray diffraction structure determination and analysis at 2.1 A resolution, multiwavelength anomalous diffraction |
| 1.1.98.2 | sitting drop vapour diffusion method, native and selenomethionine-labeled FGD1 are successfully crystallized by vapor diffusion, with the crystals diffracting to 2.1 A resolution |
| 1.1.98.2 | structure of the enzyme is determined by X-ray crystallography both in its apo state and in complex with F420 and citrate at resolutions of 1.90 and 1.95 A, respectively. The structure reveals a highly specific F420 binding mode, which is shared with several other F420-dependent enzymes. The competitive inhibitor citrate occupies the substrate binding pocket adjacent to F420. Modeling of the binding of the glucose 6-phosphate substrate identifies a positively charged phosphate binding pocket and shows that glucose 6-phosphate, like citrate, packs against the isoalloxazine moiety of F420 and helps promote a butterfly bend conformation that facilitates F420 reduction and catalysis |
