Figure 1
From: Structural basis for the membrane association of ankyrinG via palmitoylation

Crystal structure of the palmitoylation domain of AnkG.
(A) Schematic drawing of the membrane excitation platform. AnkG binds to the plasma membrane via s-palmitoylation, tethering ion channels and the cytoskeleton to the complex. (B) Crystal structure of the reduced form of AnkG (R1-R5). The dual conformation of the Cys side-chain is shown as sticks. Ca2+ is shown as a green sphere. Orientations of the repeats (R1-R5) are indicated. (C) Structure (stick models) and 2Fo-Fc maps of Ca2+ (green sphere) and its surroundings. The maps are contoured at 1.5 σ. Red balls depict oxygen atoms of water molecules. Yellow dashed lines depict polar contacts. (D) Structural comparison of AnkG and AnkB. AnkG-apo depicts the reduced form of AnkG. AnkB-AS depicts AnkB in complex with the auto-inhibitory segment (AS) of AnkR (pdb code # 4RLV)23, though the AS peptide is not shown. AnkB-Nav depicts AnkB in complex with the peptide fragment of the voltage-gated Na+ channel (Nav) (pdb code # 4RLY)23. Side-chains that interact with the regulatory peptide are shown as sticks. The yellow surface depicts the structure of the Nav peptide.