Fig. 2: ENT engages three hRpn13 Pru protomers of the crystal lattice.
From: An adaptive peptide-binding site in ubiquitin receptor hRpn13 revealed by structural studies
a, b Structural comparison of (a) ENT and (b) hRpn2 interactions with hRpn13 P40, S90 and W108. Coloring follows that of Fig. 1. c, d Expanded view of hRpn13 Pru complexed with ENT as in panel (a) but with display of an oxygen from a bound water molecule (red and labeled) with hydrogen bonds indicated (black line) and hydrogen bonds involving K42 Nε. A hydrogen bond between native T2 and non-native cG is also indicated. The image in panel (d) is rotated by 90° relative to that in panel (c). e, f Structure of ENT bound at the interface of three Pru molecules (labeled Pru-A, Pru-B and Pru-C) in the crystal lattice (Pru-C omitted for clarity). An expanded view in panel e highlights interactions between ENT and Pru-A (purple) and Pru-B (blue). Ubiquitin (yellow) and hRpn2 (green) are included in panel (f) by overlay of PDB 6OI4 with Pru-C hidden for clarity. The ENT molecules from the Pru-B and Pru-C asymmetric units are also hidden.
