Figure 9: Structure weighted sequence alignment of PatA with eukaryotic/prokaryotic acyltransferases.

(a) The protein sequences were extracted from UniProt accession numbers A0QWG5 from M. smegmatis (PatA_Msmeg); P24205 from Escherichia coli (MSBB_ECOLI); O06659 from Shigella flexneri (MSBB2_SHIFL); P0ACV0 from E. coli (HTRB_ECOLI); P45239 from Haemophilus influenzae (HTRB_HAEIN); P10349 from C. moscata (GPAT_CUCMO); Q43869 from Spinacia oleracea (GPAT_SPIOL); P0A7A7 PlsB from E. coli (PLSB_ECOLI); Q7UBC6 PlsB from S. flexneri (PLSB_SHIFL); O80437 from Arabidopsis thaliana (GPAT6_ARATH); O15228 from Homo sapiens (DHAPAT_HUMAN); Q8L7R3 from Arabidopsis thaliana (LPCT1_ARATH); Q99943 from H. sapiens (PLCA_HUMAN); and Q53EU6 from H. sapiens (GPAT3_HUMAN). Conserved positions are shown in black and grey background. Conserved hydrophobic residues are indicated with an h. The secondary structural elements corresponding to the 3D structure of PatA are shown above the alignment. Catalytic amino acids and those involved in palmitate binding are indicated as asterisks and black circles, respectively. (b) Structural similarity of M. tuberculosis H37Rv and M. smegmatis mc²155 PatA. Catalytic amino acids are indicated as asterisks. Amino acids involved in palmitate and pantotheinate binding are indicated as black and white circles, respectively. Residues proposed to interact with PIM₁ and PIM₂ based on the dockings are shown as white and black triangles, respectively. Amino acids mutated are underlined.