Figure 6: Comparison of simulation and fluorescence data with the crystal structure of the Ops*–arrestin-1 complex.
From: C-edge loops of arrestin function as a membrane anchor
(Left) Superimposition of the Ops*–arrestin-1 fusion complex crystal structure (green, PDB ID: 4ZWJ) to a sampled C-edge conformation during MD simulation (grey). Coloured horizontal lines indicate the positions for individual lipid atoms: grey lines: C=O based on the OPM database, red line: carbon 5 (C5) based on MD, brown line: phosphate atoms based on MD. (Right) Distance and fluorescence maps, derived from all-atom simulation and site-directed fluorescence experiments, respectively. Distances are depicted for a sampled C-edge conformation which was selected based on the best fit to the arrestin in the Ops*–arrestin-1 fusion complex structure with a RMSDC-domain_arrestin of 1.54 Å (calculated over all backbone atoms). The colour spectrum (0 to 20 Å) corresponds to the distance of the C-alpha carbon (VdW representation) of residues on arrestin to phosphate atoms (relates to the position of the spin label in N-tempoyl-palmitamide) and C5 atoms (relates to the position of the spin label in 5-doxyl stearic acid). The quenching data are coloured according to the degree of quenching (0 to 30%). The white asterisk indicates instances of negative quenching (see text for details).
