Fig. 1: Structure of yeast Nse2/Smc5 in complex with the E2-SUMO thioester mimetics.
From: Structural basis for the E3 ligase activity enhancement of yeast Nse2 by SUMO-interacting motifs
a Schematic representation of the engineered short form of Nse2 and Arm/Smc5 coiled-coil. b Multiple-turnover SUMOylation reactions using Nse2/Arm-Smc5 and shortNse2/Arm-Smc5. SDS-PAGE represents one of three technical replicates. c Side views of the shortNse2/Arm-Smc5 E2-SUMOD SUMOB complex. Each subunit is color coded. The crystal asymmetric unit contained one complex composed of Smc5/Nse2short, Ubc9-SUMOD thioester mimetic and SUMOB. d Side views of the structural alignment of shortNse2/Arm-Smc5 E2-SUMOD SUMOB complex with Nse2/Arm-Smc5 apo complex (3HTK). Both structures were aligned using the Arm/Smc5 coiled-coils domains. The superimposition reveals a major conformational change of loop SIM1 to interact with SUMOD and the C-terminal tail of Nse2 (named SIM2) to interact with SUMOB.
