An inhibitory mechanism of AasS, an exogenous fatty acid scavenger: Implications for re-sensitization of FAS II antimicrobials
Fig 5
Structural characterization of AasS complexed with its inhibitor C10-AMS.
A. Linear presentation of full-length AasS enzyme composed of two domains. The large domain AasS_N (residues 1–424) is connected by a short linker (residues 425–430) with the compact small domain, AasS_C (residues 431–533). Ribbon illustration (B) and surface structure (C) of AasS hexamer liganded with C10-AMS inhibitor. The AasS hexamer (130 x 140 x 65 Å) essentially behaves as a trimer of dimers, in which the subunit of monomer is numbered from I, II, …, to VI. The dimer interface was highlighted with a red arrow, and the trimer interface was indicated with a blue arrow. The AasS top view (130 x 140 Å, in upper panel) was rotated 90° counter-clockwise, giving its front view (65 x 140 Å, in bottom panel). The N-terminal domain of AasS was colored blue for AasS_N (or magenta for AasS’_N), and the C-terminal domain of AasS was displayed in powder blue for AasS_C (or light pink for AasS’_C).