Figure 1: Structure of ubiquitylated-Rpn10.
From: Structure of ubiquitylated-Rpn10 provides insight into its autoregulation mechanism
(a) Structure of Ub-Rpn10. Ub (orange) and Rpn10 (purple). (b) The refined model of the isopeptide linkage between Rpn10-K84 and Ub-G76 is shown with a Sigma-A mFo-DFc simulated-annealing omit map contoured at 2.0 σ units. (c) Electrostatic surface representation of the ubiquitylation site vicinity. The surface is coloured according to the electrostatic potential (±15 kT) and calculated in the absence of Ub with the program ABPS. (d) Ball-and-stick model showing the interactions between Ub and the vWA domain at the ubiquitylation site. The orientation is the same as in c. (e) Structural alignment of the interaction area surrounding K84 in Rpn10 from S. cerevisiae (purple) and from S. pombe (blue) shows that the two proteins share similar binding characteristics (supplementary Fig. 1).
