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. Author manuscript; available in PMC: 2020 Jul 24.
Published in final edited form as: Science. 2019 Mar 29;363(6434):1418–1423. doi: 10.1126/science.aav7541

Fig. 4. Side-chain steric packing at PL5’s symmetric helix-helix interface.

Fig. 4.

(A) The pairwise interaction of helices, symmetrically repeated, provides the primary stabilization for PL5. (B) High geometric complementarity of interacting residues across the helix-helix interface, roughly in layers: the a/g and e/g layers. (C and D) Axial view of side-chain packing of individual layers. (E) A potential stereochemical code required for pentameric assembly. At the e/d layer, the Cα-Cβ bond vector of each amino acid points outward from the helix-helix interface (βout), whereas the Cβ-Cγ bond vector faces inward (γin). This suggests that a heavy atom (e.g., N, C, O, S) at the gauche+ position is required for tight interhelical packing. (F) In the a/g layer, the opposite is true; the Cα-Cβ bond vector points inward (βin) and the Cβ-Cγ bond vector faces outward (γout).