Figure 4
Structural model of the FusB•EF-GC3 complex.
(a) The complex of FusB (green) bound to EF-GC3 (blue), determined by docking the crystal structures of the proteins informed by NMR CSPs, RDCs and PREs. Residues showing significant CSPs are shown as red sticks. The position of domain III of EF-GC3 is taken from the 2XEX crystal structure as signal broadening meant that no data to restrain the position of this domain could be obtained. (b) The correlation between amide RDC measurements in secondary structure regions of EF-GC3 bound to FusB and those calculated from the complex structure (N = 52). (c) Correlation between amide 1H PREs measured in EF-GC3 bound to FusB-R19C-MTSL (red bars) and those calculated from the complex structure (blue line) (N = 123). (d,e) PREs to FusB-R19C-MTSL (FusB shown as a cartoon, R19 as magenta sticks) in EF-GC3, shown as a cartoon in (d) and a surface representation in (e). Residues with Iox/Ired > 0.9 are shown in blue, 0.7–0.89 in cyan, 0.5–0.69 in green, 0.3–0.49 in yellow, 0.1–0.29 in orange and <0.1 in red. Residues for which there was no PRE data are shown in grey.
