Extended Data Fig. 6: Structural comparison of the Tim17-Mgr2 complex and the Sec translocon.

a, Surface presentations of Tim17-Mgr2 in a side view (left) and a cutaway side view (right). The lateral opening between Tim17 and Mgr2 in the lower half of the complex is outlined by black lines. The translocation pathway inside the complex is outlined by green lines. The restriction residues are colored green. b, Hydrophobicity distribution along the Tim17-Mgr2 translocation pathway. c, Charge distribution along the Tim17-Mgr2 translocation pathway. d, Surface presentations of the Sec translocon (PDB ID: 8RJC), shown in a side view (left) and a cutaway side view (right). The restriction (pore ring) residues are colored green. e, Hydrophobicity distribution in the Sec channel. f, Charge distribution in the Sec channel. g, Superimposition of the restriction residues in the Tim17-Mgr2 pathway and the Sec channel. Tim17, Mgr2, and Sec (PDB ID: 6ITC) are colored brownish pink, gold, and grey, respectively. The restriction residues of Tim17-Mgr2 and Sec are shown as balls and sticks, and colored forest green and grey, respectively. h, The substrate exit site of Tim17-Mgr2. The translocation direction toward the β sheet of Tim44 is indicated by a black arrow. i, same as h, except showing the hydrophobicity distribution of the exit site. The polypeptide substrate is represented as a curved line.