Figure 2
Identification of residues that form the binding interface in EF-GC3 and FusB and mapping of these binding sites onto the corresponding protein structures.
(a) Combined 1H and 15N chemical shift changes in EF-GC3 upon binding FusB calculated only for those residues assigned in both apo and FusB bound spectra. CSPs considered significant (>1.0 ppm) are shown in red. Residues for which peaks disappear from the spectrum upon complexation are shown as yellow circles. (N = 155) (b,c) Residues showing significant CSPs are indicated in red on 180° rotated views of the crystal structure of apo EF-GC3 displayed as a ribbon diagram (b) and in surface view (c). Significant perturbations predominantly form a patch on one side of domain IV and represent the primary site of interaction with FusB. (N = 167) (d) Combined 1H and 15N chemical shift changes in FusB upon binding to EF-GC3 using direct measurement for residues assigned in both spectra and minimal shift changes for all residues assigned only in the apo spectrum assuming the closest bound state peak represents the same residue. CSPs considered significant (>0.6 ppm) are shown in red. (e,f) Residues showing significant CSPs are indicated in red on the crystal structure of apo FusB as a ribbon diagram (e) and in surface view (f). Significant perturbations predominantly form a patch on one side of the C-terminal domain and represent the primary site of binding to EF-G.
