Fig. 3: Structure and conformational flexibility of full-length Pfs48/45.

a, A composite model of Pfs48/45 in the Pfs48/45-scTB31F:RUPA-44:RUPA-58:RUPA-154 complex reveals an extensive interface between D1 and D2. The 5-aa linker (residues 290–294) between D2 and D3 is highlighted in red. b, The flexible linker between D2 and D3 results in continuous rotation of the D1–D2 region versus D3 by ~7°, as revealed by 3D variability analysis. c, Top, a ccomparison of Pfs48/45 models from the Pfs48/45-scTB31F:RUPA-44:RUPA-58:RUPA-154 complex (left), the Pfs48/45-scTB31F:RUPA-44:RUPA-58 complex (middle), and the Pfs48/45:10D8 cocrystal structure (right, PDB ID: 7ZXG) reveals considerable changes in angles between D2 and D3. Bottom, D3 displacement between the Pfs48/45-scTB31F:RUPA-44:RUPA-58:RUPA-154 complex (purple), the Pfs48/45-scTB31F:RUPA-44:RUPA-58 (magenta) complex, and the Pfs48/45:10D8 cocrystal structure (pink) is depicted by red dashed lines. The angle and displacement between domains was calculated with angle_between_domains command in Pymol³⁶. The red dots and lines denote the centers of mass of individual domains and distances between them, respectively. d, Backbone r.m.s.d. between Pfs48/45 in the Pfs48/45-scTB31F:RUPA-44:RUPA-58:RUPA-154 complex and the Pfs48/45:10D8 cocrystal structure. Models were aligned either to D2 (left) or D3 (right) using PyMOL³⁶, and r.m.s.d. values were calculated using UCSF Chimera³⁷.