Fig. 5: Conserved donor strand complementation across cannulae forming subunits. | Nature Communications

Fig. 5: Conserved donor strand complementation across cannulae forming subunits.

From: Donor strand complementation and calcium ion coordination drive the chaperone-free polymerization of archaeal cannulae

Fig. 5

a multiple sequence alignment (MSA) of mature CanA, CanX, and Hyper2 sequences (Jalview, Clustal coloring). Red stars denote regions where CanA loop/domain insertions were removed for visual clarity. Red arrows highlight conserved residues that interact with calcium in type I, II, and III coordination centers. Arrows below the MSA denote secondary structure elements color coded according to the monomer cartoon representation in (b); b Illustration of the cannula donor strand complementation mechanism shown here for CanX: the N-terminal strand A of subunit j docks into the surface exposed hydrophobic groove defined by the region between strands B and K of subunit i; c–e zoomed-in renditions of the donor strand (stick representation) docking into the respective B/K grooves for CanX, CanA and Hyper2, respectively. Donor sequences above (c–e): hydrophobic residues docked into complementary pockets highlighted in bold; residues forming sidechain-mediated intermolecular hydrogen bonds shown in red; proline directing the N-terminus towards the “lattice contact” underlined.

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