Overall structural comparison of <i><sup>Dm</sup></i>cN-IIIB bound to m<sup>7</sup>G with <i><sup>Mm</sup></i>cN-IIIA bound to UMP.

<p>Superposition of <i><sup>Dm</sup></i>cN-IIIB (HAD core in white; cap domain in red) and cN-IIIA (HAD core in grey; cap domain in blue) showing the overall structural similarity of both enzymes. Note that the cap domain of cN-IIIB is shifted by 4 Å when the structures are superposed <i>via</i> their the HAD core. Thus, the substrate-bound cN-IIIA adopts a closed conformation while the product-bound cN-IIIB represents an open conformation. A movie of the trajectory from the open-to-closed state is shown in <b><a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0090915#pone.0090915.s005" target="_blank">Movie S1</a></b>.</p>