Extended Data Fig. 5: Secondary structure diagram and sequence alignment of human GPAT1 with mammalian and bacterial GPAT orthologs.

The protein sequences were extracted from UniProt accession numbers Q9HCL2 from Homo sapiens (GPAT1_HUMAN); Q61586 from Mus musculus (GPAT1_MOUSE); P97564 from Rattus norvegicus (GPAT1_RAT); P0A7A7 from Escherichia coli (PLSB_ECOLI, amino acids 50–805); and P44857 from Haemophilus influenzae (PLSB_HAEIN, amino acids 30–804). Protein sequences are denoted as conserved sequences (*), conservative mutations (:), semi-conservative mutations (.), and non-conservative mutations (no symbol). Secondary structural elements corresponding to the 3D structure of human GPAT1 are shown above the alignment, with structural domains colored in the same scheme as Fig. 1. Black dashed lines are residues that were not included in the cryo-EM construct, whereas the colored dashed lines are regions that were included in the construct but not modeled in the structure. Cylinders and arrows represent α-helices and β-strands, respectively. Membrane-associating sequences are highlighted in gray. Catalytic amino acids are in red text. The four conserved sequence blocks are enclosed in black boxes.