Fig. 6
From: Epsin and Sla2 form assemblies through phospholipid interfaces
Human ENTH forms a thermally stable hexamer with a predicted membrane-binding interface. a SAXS modeling of human ENTH in the presence of PIP2. SAXS data recorded for human ENTH in solution are shown (gray circles) along with a fit to the rigid-body model refined against the SAXS data with P3 symmetry using CORAL (orange solid line). Experimental errors are from counting statistics on the Pilatus 2M detector and propagated through the data reduction process as standard errors in the scattering intensities. The χ2 for the fit is 1.05. The inset shows the dimensionless Kratky plot representation of the SAXS data and the same fit. b Backbone and surface representation of the SAXS refined rigid body model. C-terminal (Ct) residues not observed in the crystal structure of the tandem domains are modeled as dummy residues by CORAL. P3 symmetry was enforced and the tandem ENTH domains with bound PIP2 used as rigid bodies. c 90° rotation of the model, demonstrating that the bound PIP2 molecules are all located on one side of the protein, consistent with a membrane-binding interface. The Thr 104 residues involved in ENTH/ENTH homodimerization are colored pink, whereas the Thr 104 residues present on the surface of the hexamer are colored green. d Hydrodynamic radius as a function of temperature measured by DLS (ENTH, S. cerevisiae, orange; ENTH/ANTH complex, S. cerevisiae, green; hexameric ENTH core, H. sapiens, blue)
