Fig. 5.

NADPH-induced conformational changes of mMICAL₄₈₉. (A) Stereo-view of the superposition of oxidized and reduced (gray) mMICAL₄₈₉. FAD molecules are drawn as sticks. The oxidized form is colored red where there are significant differences between the structures, whereas blue parts are super-imposable [significance level is defined by default criteria of the program escet (37)]. (B and C) Cavities in the oxidized (B) and reduced (C) forms drawn as chicken wire (red, oxidized; cyan, reduced). Both have identical depth slab and orientation, centered on the MO/FAD-binding domain interface (protein atoms are omitted for clarity). The asterisk marks the increase of cavity volume in the reduced form (channel). (D) The solvent-accessible surface of mMICAL_489^* with the channel entrance highlighted in red (orientation is as in Fig. 1B). Potential NADPH-binding residues are colored cyan. A blue dotted circle marks the patch of basic electrostatic potential. The orientation is as in Fig. 1B.