Fig. 3: Structural basis for Uba7/ISG15 molecular recognition. | Nature Communications

Fig. 3: Structural basis for Uba7/ISG15 molecular recognition.

From: Cryo-EM structures of Uba7 reveal the molecular basis for ISG15 activation and E1-E2 thioester transfer

Fig. 3: Structural basis for Uba7/ISG15 molecular recognition.The alternative text for this image may have been generated using AI.

a Relative rotations of ISG15(a) and the Uba7 FCCH domain compared to their counterparts in the Uba1/Ub(a) structure (PDB ID: 4II2). Uba7 and Uba1 were superimposed and the relevant domains/proteins are shown as cartoons and colored as labeled. b The Uba7-UBE2L6-ISG15(t)/ISG15(a) complex is shown as a cartoon representation (left) with a magnified view of Uba7/ISG15(a) interface I (right). Hydrogen bonds are indicated by dashed lines. c Uba7-ISG15 thioester formation assays of the indicated mutants at the Uba7/ISG15(a) site I interface. d Unique residues proximal to the polar patch of ISG15 (gold) participate in a distinct network of contacts to unique residues in Uba7 (gray) compared to the Uba1/Ub (spring green/cadet blue) (PDB ID: 6DC6) interface. e The Uba7-UBE2L6-ISG15(t)/ISG15(a) complex structure is shown as a ribbon representation as in panel b, with a magnified view of Uba7/ISG15(a) interface II. f Uba7-ISG15 thioester formation assays of the indicated mutants at the Uba7/ISG15(a) site II interface. g The Uba7-UBE2L6-ISG15(t)/ISG15(a) complex structure is shown as a ribbon representation as in panel b, with a magnified view of Uba7/ISG15(a) interface III (CL: cross over loop). h Uba7-ISG15 thioester formation assays of the indicated mutants at the Uba7/ISG15(a) site II interface. Data presented in c, f, and h are represented by mean ± SEM with three independent technical replicates labeled above and individual replicates shown as black circles. The source data are provided in the source data file.

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