Extended Data Fig. 10: Comparison of the GPAT1 cryo-EM structure with the AlphaFold model.
From: Structural basis of the acyl-transfer mechanism of human GPAT1
a-d, Overlays of the GPAT1–2-oxohexadecyl-CoA cryo-EM structure (teal) with the AlphaFold model (UniProt ID Q9HCL2, firebrick red) in Cα ribbon representation from four different views. The unmodeled regions of the cryo-EM structure are also hidden in the AlphaFold model for clarity. e, Differences observed between the cryo-EM structure and the predicted AlphaFold model at the membrane gate helices, α12 and α9, as well as at selected side chains in the catalytic site and the membrane gate pocket. The highlighted residues, R278, R279, R328, and H363 are shown in sticks. Polar interactions between R278 and R328 observed in the cryo-EM structure are indicated by dashed lines. The small molecules, 2-oxohexadecyl-CoA in the catalytic site and palmitoyl-LPA in the membrane gate pocket resolved in the cryo-EM structure are shown in green and light gray sticks, respectively.
