Figure 4: NMR solution structure of lys11-linked SUMO-2 dimer.
From: Structural insight into SUMO chain recognition and manipulation by the ubiquitin ligase RNF4
(a) Superposition of the NMR ensembles for distal (SUMO-2 ΔN11, cyan) and proximal subunits (SUMO-2 ΔGG, green) highlights the structural similarity of the two domains. (b) Cartoon representation for the superposition of SUMO-2 dimer subunits (distal in cyan and proximal in green) and previously determined SUMO structures, namely SUMO-3 from 2RPQ (marine)31 and SUMO-2 from 1WM3 (yellow)41. The SUMO-2 domains within the SUMO-2 dimer are highly similar to reported structures for individual SUMO domains, as they superpose with an r.m.s.d. of 1.7 Å over 72 backbone atoms for SUMO-3 and 1.6 Å over 75 residues for SUMO-2. (c) The NMR ensemble of 20 structures for the individual SUMO domains within the SUMO-2 dimer superposed over equivalent atoms in the distal domains (SUMO-2 ΔN11, cyan) to illustrate the absence of a preferred relative orientation of the two SUMO-2 domains (d) The NMR ensemble for the SUMO-2 dimer superposed over equivalent atoms in the proximal domain (SUMO-2 ΔGG, green).
