Fig. 2: Architecture of the XPF helicase-like module and coupling with the catalytic module. | Nature Communications

Fig. 2: Architecture of the XPF helicase-like module and coupling with the catalytic module.

From: Cryo-EM structures of the XPF-ERCC1 endonuclease reveal how DNA-junction engagement disrupts an auto-inhibited conformation

Fig. 2

a View of the XPF–ERCC1 structure showing the helicase-like module (HLM as surface rendering) contacts the XPF nuclease domain (gold ribbon cartoon) at two interfaces (dashed red boxes). Domains are coloured according to the scheme used in Fig. 1. b, c Close-up view of interaction interfaces overlaid with the composite cryo-EM map. Selected residues are displayed as sticks and coloured by heteroatom, blue—N, Red—O. b The hydrophobic interaction interface between XPF RecA2 (blue) and XPF nuclease domain (gold). c Interaction of XPF helical domain residues 273–275 (green) with the XPF nuclease domain (gold). d the XPF–ERCC1 HLM (surface rendered) contacts with the ERCC1 (HhH)2 domain at a single interface (dashed red box). e Interaction of XPF helical domain helix α13 (green) and the ERCC1 (HhH)2 domain close to its dsDNA-binding residues (pink). f Two orthogonal views of the XPF–ERCC1 structure with XL-MS distance constraints overlaid. Distances within the allowed Cα–Cα cut-off distance of 30 Å are displayed in blue, distances greater than this cut-off displayed in red. Blue dotted line indicates a cluster of allowed distances between the XPF helical and ERCC1 (HhH)2 domains. g Cartoon schematic representing inter-domain cross-links detected by mass spectrometry. Each black line indicates a single unique cross-link between residues in different domains. Domains within the pink ellipsoid form the XPF HLM, whereas domains within the XPF CM and ERCC1 are within the pale blue ellipsoid.

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