Extended Data Fig. 7: Alphafold-predicted models of LPD-3 complex subunits. | Nature

Extended Data Fig. 7: Alphafold-predicted models of LPD-3 complex subunits.

From: Structural basis of lipid transfer by a bridge-like lipid-transfer protein

Extended Data Fig. 7

a, The Alphafold-predicted model of LPD-3. β-strands are coloured gold, α-helices are pink, and coils are green. b, The Alphafold-predicted structure of LPD-3, coloured as in (a), is superposed on the experimental model of LPD-3 (teal), revealing a high degree of structural similarity. The structures exhibit an overall α-carbon RMSD of 5.6 Å. c, The superposed structures of the LPD-3 experimental model (teal) and the Alphafold-predicted structure (gold) are shown in licorice representation. The Cγ atoms of the residues that form the ionizable track are shown as spheres, highlighting the conserved orientation of these residues in the experimental and predicted structures. d, The Alphafold-predicted model of Spigot, coloured as in (a). e, The Alphafold-predicted model of LTAP2, coloured as in (a).

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