Skip to main content
. 2016 Jul 7;99(1):174–187. doi: 10.1016/j.ajhg.2016.05.028

Figure 3.

Figure 3

Structural Topology of the Mutations in Sec61

The cryo-EM based models of translocons translating hydrophilic peptide with opened pore (PDB: 4CG5) and translating peptide inserted to membrane possessing a pore sealed by a plug domain (PDB: 4CG6) were used for illustration. Regions containing mutations are depicted with cartoon representation, namely plug domain (p.Val67Gly) in magenta and TM5 (p.Thr185Val) in orange. Mutated residues are highlighted as dots and/or sticks.

(A) Overall structure of Sec61 and location of the mutated residues.

(B) Orientation of the mutated residues in the Sec61 structure with opened translocation pore (left) and with pore sealed by a plug domain (right).

(C) Left: constriction ring formed by apolar residues represented by green (TM2, TM7, and TM10) and orange (positioned at TM5 near Thr185 residue) spheres; mutated residues are shown as red spheres. Right: detail of TM5 illustrating hydrogen bonding of hydroxyl Thr185 with carbonyls of Leu181 and Phe182.