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Fig. 8 | BMC Biochemistry

Fig. 8

From: Structural similarities and functional differences clarify evolutionary relationships between tRNA healing enzymes and the myelin enzyme CNPase

Fig. 8

SAXS analysis of Bf and ScTrl1 PNK/CPDases. a Scattering curves from monomeric Bf (blue) and ScTrl1 (red) PNK/CPDases and the ScTrl1 CPDase domain (green). The curves have been displaced for clarity. b Guinier plots for the samples in (A), plotted between 0.8 < sRg < 1.3. The curves have been moved in the y dimension for clarity. c Distance distribution functions for the samples shown in (A). d Dimensionless Kratky plots. The cross marks the expected peak position for a folded globular protein (x = 1.732, y = 1.1). BfPNK/CPDase is most flexible of the proteins. e-g Ab initio 3D models for BfPNK/CPDase, ScTrl1 PNK/CPDase, and the ScTrl1 CPDase domain, respectively. The DAMMIF bead model is shown by spheres and the GASBOR chain-like model as a surface in each panel. h Comparison of the 2-phase MONSA model of ScTrl1 PNK/CPDase (left) with the earlier published SAXS structure of full-length MmCNPase (right) [28]. The positions of the N-terminal PNK domain and the C-terminal CPDase domain are indicated for both proteins. See Table 3 for the chi2 values corresponding to the fit between the raw data and the models

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