Fig. 3
NMR-derived structures of Mg2+-bound GCAP5 (PDB entry 7M2M). (A) Ensemble of the 10 lowest-energy NMR structures. Structural statistics are listed in Table 1. (B) Average main chain structure of GCAP5 and (C) the same view rotated by 180° showing four EF-hands (colored as in Figure 1) packed in a globular arrangement very similar to what is seen for Ca2+-bound GCAP1.9 (D) Overlay of the main chain structure of GCAP5 (cyan) and the crystal structure of GCAP1 (red). The secondary structural elements are labeled as defined in Figure 1. The Ca2+ switch helix (α10) is colored purple. Cys15 and Cys17 side chain atoms are colored yellow. Bound Mg2+ is colored orange. The N-terminal myristoyl group is colored magenta. Side chain atoms of residues at the dimer interface (H18, Y21, M25, F72, and V76) and Mg2+ binding site (D63, D65, and D67) are indicated as sticks. (D) Overlay of main chain structures of Ca2+-bound GCAP1 (red) and Ca2+-free, Mg2+-bound GCAP5 (cyan).