Fig. 2: Molecular insights into UBE2E1-mediated ubiquitination without E3.
From: Structure-guided engineering enables E3 ligase-free and versatile protein ubiquitination via UBE2E1
a Detailed interactions of hexapeptide with UBE2E1 residues. The intermolecular hydrogen bonds are indicated with yellow dashed and the residues are shown as sticks with the same color code as in Fig. 1c. b UBE2E1 D136 residue poised to activate the modeled lysine residue’s nucleophilicity. c Interaction diagram between UBE2E1 and SEDTB1-derived peptide. Intermolecular hydrogen bonds and hydrophobic interactions are indicated with yellow dashes and arrows, respectively. d The proper distance between the receptor lysine and glycine at the corner of “L-shaped” hexapeptide is necessary for ubiquitination. e Engineered Ubch5c enabled site-specific ubiquitination in an E3-free manner. Gel images shown in (d) and (e) are representative of independent biological replicates (n = 2). Source data are provided as a Source Data file.
