Fig. 3
From: A ubiquitin-like domain is required for stabilizing the N-terminal ATPase module of human SMCHD1

Superposition of SMCHD1 to GHKL-ATPases ParE44 and GRP94. a Superposition of topoisomerase ParE44 (cyan) with bound DNA (red) (pdbidcode:5J5Q; RMSD 3.5 Å, 484 Cα’s) to SMCHD1. b Close-up view of superimposed DNA (red) in the cavity of SMCHD1. The disordered Asp/Glu-loops from the transducer domains of SMCHD1 are represented by dotted lines. In the current conformation, these loops would likely form steric as well as electrostatic repulsive interactions with a negatively charged client like DNA. c Superposition of heat-shock protein GRP94 (transparent blue) with polypeptide (magenta) bound at the client-binding site (pdbidcode:5ULS, RMSD 4.0 Å, 541 Cα’s) to SMCHD1. d Close-up view of the superimposed client mimic peptide from GRP94 in the cavity of SMCHD1. SMCHD1 is colored as in Fig. 1