Fig. 5
Structural comparison of interfacial amino acid residues in different organisms. A Sequence alignment of interfacial amino acid residues in different organisms. Some amino acid residues at the interface of two adjacent hexamers in human PRPS2 filament are conserved. The conserved amino acid residues are shown in red. B Structural comparison of interfacial amino acid residues between hPRPS2 (blue) and E. coli type A filament PRPS (7XMU) (yellow). The human PRPS2 filament is the same as E. coli PRPS type A filament, and the amino acid residues involved in the hexamer interconnection are conserved. C Structural comparison of interface amino acid residues between human PRPS2 (blue) and E. coli type AADP+AMP filament PRPS (7XMV) (green). The position of the amino acids involved in the interconnection of hexamers are highly similar. D Structural comparison of interface amino acid residues between human PRPS2 (blue) and E. coli type B filament PRPS (7XN3) (gray). Compared with E. coli type B filament PRPS (7XN3), the position of amino acid residues involved in the interconnection of hexamers has shifted. The amino acid residues in E. coli type B filament PRPS (7XN3) are labeled with ‘. (E) Structural comparison of interface amino acid residues between hPRPS2 and hPRPS (2HCR). The amino acid residues in hPRPS (2HCR) are labeled with ‘