Fig. 7.
Structures of the E447A mutant of MtbFadE5 in complex with C18CoA and its substrate binding cavity. (A) Cartoon representation of the dimer. Individual subunits are shown in yellow and red. (B) The 2Fo–Fc electron density map for C18CoA contoured at 1.0σ. (C) Equivalent 2Fo–Fc electron density map for C18CoA contoured at 0.6σ. (D) Superimposition of the MsFadE5 complex (green) and MtbFadE5 complex (red and yellow). (E) Superimposition of the substrate binding cavities in the MsFadE5 complex (green) and the MtbFadE5 complex (yellow). Residues along the substrate binding cavity walls that differ between the two structures are shown in stick models. The C18CoA in MsFadE5 is in pink, and C18CoA in MtbFadE5 is in blue.