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. Author manuscript; available in PMC: 2018 Feb 16.
Published in final edited form as: Mol Cell. 2017 Feb 2;65(4):699–714.e6. doi: 10.1016/j.molcel.2017.01.008

Figure 1. Uba1-Ubc15/Ub structure reveals a distinct Ub E1 binding mode.

Figure 1

(A) E1-E2 Ub thioester transfer assays for the indicated Uba1-E2 pairs.

(B) Uba1-Ubc15 thioester transfer assay under endpoint conditions, prepared in the presence and absence of reducing agent.

(C) Cartoon of the Uba1-Ubc15/Ub complex with Uba1 domains color-coded and labeled.

(D) Uba1 from the Uba1-Ubc15 structure is colored as in C and Uba1 from the Uba1-Ubc4 structure (PDB: 4II2) is colored gray. Uba1 adenylation domains superimposed (RMSD=0.207 Å). Domain rotations indicated with arrows.

(E) The UBC domains of Ubc15 (cyan) and Ubc4 (gray) were superimposed and the structures are shown as ribbons.

(F) Uba1-Ubc15 (left) and Uba1-Ubc4 (right) structures with Uba1 atoms contacting E2 colored by domain, as in C.

(G) Ubc15 and Ubc4 Uba1 binding modes. The adenlyation domains were superimposed and colored as in D and the E2s are shown as cartoons and colored as in E.

See also Table 1 and Figure S1.