Comparison of PUS1 / RNA complex structures.

(a) Superposition and side-by-side comparison of PUS1_D134A / RNA complex (colored protein backbones) solved in crystallographic space group C2 and wild type PUS1 / RNA complex (grey protein backbones) solved in an unrelated, P6₁22 space group. In both structures, two monomers of the enzyme are independently bound in a symmetric arrangement to an RNA duplex that is generated via crystallographic 2-fold symmetry. (b) Model and electron density for wild type PUS1 and the region of the RNA containing the 5’ 5-fluorouracil base. A 2Fo-Fc map (gray) is contoured at 1s. In the corresponding refinement, the base is estimated to display greater than 90% occupancy of the unflipped conformation, as modeled and shown.

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