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Figure 5
Structural conservation over the Sm fold. (a) Superposition of the Cα trace of all seven Sm proteins, with helix H1 coloured dark red and the β-strands in shades of cyan and green. A dashed circle indicates the Cα position of the conserved hydrophobic residue in H1. (b) The side chain-to-side chain contacts between the conserved residue in H1 and other conserved residues within the hydrophobic belt. This example shows contacts between Leu11 (in a dashed circle) in H1 of SmF and other residues of SmF (brown) and SmE (yellow). |
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