Figure 5
Structural alignment of PatF (green) and DMATS (cyan) highlighting the key residues involved in DMATS-DMAPP binding and their absence in PatF. Lys187 of DMATS forms a salt bridge to the phosphate O atom of the DMAPP mimic (2.67 Å), while Asp178 forms a stabilizing interaction with Arg100, which in turn forms a salt bridge to the DMAPP mimic. In PatF, Lys187 and Asp178 correspond to Met136 and His125, respectively. These residue changes would abolish these DMAPP-binding interactions.  [article HTML]