Fig. 2: MAX2–HTL7 is closed with the GR24 D-ring trapped in its active site. | Nature Communications

Fig. 2: MAX2–HTL7 is closed with the GR24 D-ring trapped in its active site.

From: Mechanism of cooperative strigolactone perception by the MAX2 ubiquitin ligase–receptor–substrate complex

Fig. 2: MAX2–HTL7 is closed with the GR24 D-ring trapped in its active site.

A Superimposition of HTL7 from our cryo-EM structure (PDB 9KKX; purple) and the open-conformation crystal structure of HTL7 (5Z8P; pink). The collapsed lid domain of our model is coloured grey, and the D-loop is coloured magenta. The catalytic triad residues are shown as sticks. The black box outlines the active site and magnified views in the following panels. B Fit of the D-ring covalently attached to H246 (H246–D-ring) in the cryo-EM density. Catalytic triad residues are shown as sticks and labelled. C Hydrophobic enclosure (mesh outline) in the open (top) and our closed (bottom) HTL7 active site. The GR24 D-ring is shown as orange spheres. Red arrows highlight the active site entrance. The collapsed lid domain is coloured grey. Catalytic triad residues are shown as sticks and labelled (top). Residues that form the hydrophobic enclosure in the closed conformation are shown as sticks and labelled (bottom). D Superimposition of catalytic triad residues in the closed and open conformations with the H246–D-ring modification added to the open conformation. Yellow dashed lines depict clashes between atoms closer than 0.6 Å. E Superimposition of catalytic triad residues in closed and open conformations. Distances between atoms are shown as dotted lines and labelled.

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