Figure 3.

Architecture of the S. pneumoniae-associated Spr1654 aminotransferase. (a) The crystal structure of the Spr1654 dimer reveals a type I aminotransferase fold. The N-terminal arm is coloured in black. The large PLP-binding domains from the A and B subunits are coloured in cyan and green, respectively. The smaller C-terminal domains are coloured in purple and yellow, respectively. The two insertions 150–164 and 212–217 that are found only in Spr1654 are coloured in blue and red, respectively. (b) Interface and active sites within the Spr1654 homodimer. The surface and the homodimer interface within one of the two subunits are coloured in cyan and wheat, respectively. The cartoon representation of the other subunit is coloured in rainbow, with the disordered region coloured in grey. The active site is indicated in one of the two subunits.