Extended Data Fig. 5: GDP/GTP structural cycle of GerdArfR1.
From: The Asgard archaeal origins of Arf family GTPases involved in eukaryotic organelle dynamics
a, (left) Crystal structure of GerdArfR1-Δ12-Q69L bound to Mg.GTP. The protein is shown with the interswitch in blue and Switch I/Switch II in light blue. Below, the nucleotide binding site of the Mg.GTP is enlarged. The N-terminal AH which is absent from the fragment crystallized, is shown schematically. (right) Crystal structure of GerdArfR1-FL-WT bound to Mg.GDP. The protein is shown with the N-terminal helix and the interswitch in pink and Switch I/Switch II in light pink. Above, the N-terminal helix is magnified and shown in two orientations rotated by 90°. Hydrophobic residues Leu3, Phe5, Leu6, Leu9 and Phe10 from the N-terminal AH of GerdArfR1 (indicated in yellow) are buried in the hydrophobic pocket formed by the tip of the interswitch and the C-terminal helix. Overall, proteins are shown with a cartoon representation, magnesium ions with a green sphere and nucleotides with a stick representation. b, Superposition of the GTP-bound and GDP-bound forms of HodArfR1. Colors are as described in part a.
