Fig. 1: Structure and conformational flexibility of hAtg3ΔN25, Δ90–190.
a Overlay of hAtg3ΔN25, Δ90–190 ten solution structures. C-terminal unstructured residues 306–314 are not shown for clarity. b Structural alignments of hAtg3ΔN25, Δ90–190 (gray) with yeast Atg3 (purple, PDB 6OJJ, left), and Arabidopsis thaliana Atg3 (violet, PDB 3VX8, right). Helix F is indicated. c H/D exchange of 15N-labeled hAtg3ΔN25, Δ90–190 at pH 6.5, 25 °C. Group I: residues with fast H/D exchange (more than 67% of resonance intensities lost within 38 min after adding D2O) are colored red. Group II: residues with slow H/D exchange (less than 67% of resonance intensities lost at ~23 h after adding D2O) are colored cyan. Group III: residues with intermediate H/D exchange (slower than Group I and faster than Group II) are colored orange. Given the structural conservation, secondary structural elements are indicated according to corresponding elements in a yeast Atg3 structure (PDB 2DYT). Source data are provided as a Source Data file. d Residues with different H/D exchange rates are mapped onto the hAtg3ΔN25, Δ90–190 NMR structure in corresponding colors as shown in (c). Residues with uncharacterized H/D exchange rates are shown in gray. Helix F is indicated, and catalytic residue Cys264 is shown in VDW.
