The overall structure of MsPrsA.

<p>Ribbon representation of the quaternary structure consisting of an hexameric arrangement (A) and of the monomer fold (B). Domains are colored in cyan (N-terminal) and green (C-terminal). The 3₁₀-helix and the flexible loop, part of the N-terminal domain, are colored in red and magenta, respectively. Flag regions (β-hairpin β2-β3, and β9-β10) are shown in yellow, and the two extremities of the disordered loop are indicated (residues 204 and 213). The acetate molecule (ACT) is shown as ball and stick and the water is represented as a red sphere. (C) Magnified view of R5P binding loop with protein residues and acetate shown as ball-and-stick and the water molecule as a red sphere; relevant interactions are indicated with black dashes. The 2Fo-Fc electron-density map has been contoured at 1.0σ level.