Fig. 4: Structure of the UBA6-FAT10 complex.
From: Structures of UBA6 explain its dual specificity for ubiquitin and FAT10
a Overall structure of UBA6 color coded according to its domains in complex with FAT10 in yellow. The NTD and CTD of FAT10 are labeled. b UBA6-FAT10 complex with UBA6 in surface representation and FAT10 in ribbon and dot representation. c Superimposition of the UBA6-FAT10 complex color coded as in (a) and the Uba1-ubiquitin complex with Uba1 in gray and ubiquitin in orange. d Hydrophobic interface between the CTD of FAT10 (yellow) and AAD (magenta)/IAD (cyan) of UBA6. Interacting residues are labeled and shown with their side chains. Parts of the FAT10 C-terminal tail (residues 159–162) are shown in all-atom representation. e Ubiquitylation (left) and FAT10ylation (right) assays of UBA6 wild-type and variants (F316A and V934A). Raw data (top) and quantification (bottom). n = 3 independent replicates, data are presented as mean values ± SD. Source data are provided as a Source Data file. f Recognition of the FAT10 C-terminal tail in all-atom representation with surrounding residues in the AAD and IAD.
