Fig. 3: Structural and selective consideration of Atsly1 mutant proteins.
From: Evolution of a plant growth-regulatory protein interaction specificity
a, AlphaFold AtSLY1 structure prediction shown in 90o rotation and with helical F-box (cyan), core helical GGF (brown) and outward-facing helical LSL domains (purple) (see also Extended Data Fig. 3a–c). Amino-acid side chains of residues targeted by substitutions in Atsly1 mutant proteins (for example, H104) are shown as sticks and labelled. The position of G84 is indicated by a sphere. The N-terminal 25 residues, which are predicted to be unstructured, are not shown. b, Mean (±s.d.) strengths of yeast 2-hybrid interactions between AtSLY1 (or indicated variants) and GAI. Red dots indicate individual values (n = 3), different letters (a, b) indicate significant difference (two-sided Student’s t-test). P = 0.0044. c, Mean (±s.d.) strengths of yeast 2-hybrid interactions between AtSLY1 (or indicated variants) and GAI. Red dots indicate individual values (n = 3), different letters (a–g) indicate significant differences (one-way ANOVA with Tukey’s test). d, AlphaFold prediction of the AtSLY1–GAI complex structure. Amino-acid residues targeted by substitutions in Atsly1 mutant proteins are shown as spheres and labelled (see also Extended Data Fig. 4e,f). N-terminal residues of SLY1 and GAI predicted to be unstructured are not shown. e, AlphaFold AtSLY1–GAI structural prediction showing H104 intramolecular contacts within AtSLY1. The H104 side chain is in van der Waals spheres and side chains for residues with atoms ≤5 Å from any H104 atom are shown as sticks. GAI is shown as a grey ribbon. All residue contacts ≤5 Å are within SLY1 and, apart from the F-box residue A49, all are within the GGF region and include W72, I75 and C76. A ‘bulge’ visible at Y107 in the helix is due to formation of a π-helix turn starting at H104.
