Figure 6: Role of the amphipathic α-helix in the proposed locking pin mechanism of calcium regulation. | Scientific Reports

Figure 6: Role of the amphipathic α-helix in the proposed locking pin mechanism of calcium regulation.

From: Calcium regulation of the human mitochondrial ATP-Mg/Pi carrier SLC25A24 uses a locking pin mechanism

Figure 6

View from the membrane of the (a) calcium-bound or (b) calcium-free states of the APC1 model. The calcium-bound regulatory domain in blue is based on PDB: 4ZCV. Residues of the blue and green clusters are displayed as colored spheres, representing the Cα atoms. Known (a) and predicted (b) interactions between residues in the different states have been indicated with dashed black lines. The calcium-free regulatory domain is based on a model in which all EF-hands of the regulatory domain are closed12. The carrier domain in grey is a comparative model based on the bovine AAC crystal structure (PDB: 1OKC)16. The amphipathic α-helix is shown in red. The α-helices are represented as cylinders. The substrates ATP-Mg and phosphate, and activating calcium ions are in sphere representations.

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