Structures of the ATP-bound CaMKI.

<p><b>A</b> Comparison of the CaMKI320-ATP complex with the apo CaMKI320. The CaMKI320-ATP complex is colored as in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0044828#pone-0044828-g001" target="_blank">Figure 1A</a>, and the apo CaMKI320 is colored in gray. The three regions where the CaMKI320-ATP complex shows substantial conformational differences from the apo CaMKI are indicated with ovals. <b>B</b> The 2<i>F</i>o-<i>F</i>c maps of the bound ATP molecules (contoured at 1σ level) in the CaMKI320-ATP, CaMKI315-ATP, and CaMKI293-ATP structures. <b>C</b> Hydrophilic interactions of ATP with the surrounding residues in CaMKI320-ATP. ATP and the interacting residues are shown with ball-and-stick models, and the hydrogen-bonding interactions are indicated with dashed lines. <b>D</b> Comparison of the CaMKI293-ATP complex and the Akt/PKB-GSK3β complex at the catalytic site. The color coding is the same as in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0044828#pone-0044828-g001" target="_blank">Figures 1A</a> and <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0044828#pone-0044828-g002" target="_blank">2D</a>. The bound ATP is shown with a ball-and-stick model. Glu66 on helix αC and Lys49 on strand β3 in CaMKI293-ATP and their equivalents (Glu200 and Lys181) in Akt/PKB-GSK3β are shown with ball-and-stick models.