Fig. 1: Structure of auto-inhibited human XPF–ERCC1 endonuclease. | Nature Communications

Fig. 1: Structure of auto-inhibited human XPF–ERCC1 endonuclease.

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

Fig. 1

a Domain architecture of XPF–ERCC1 colour coded by domain. XPF: RecA1 (blue), helical (green), RecA2 (pink), nuclease (gold) and (HhH)2 (dark grey). ERCC1: NLD (orange) and (HhH)2 (light grey). Residue numbering indicates domain boundaries and dotted arrows indicate dimerisation interfaces. Two insert sequences within RecA2 are shown in white embellishing the RecA domain fold. Grey lines define the helicase-like module (HLM) and catalytic module (CM). b SDS-PAGE gel of purified recombinant XPF–ERCC1 used for cryo-EM studies. c Two orthogonal views of the composite XPF–ERCC1 cryo-EM map ranging from a global resolution of 3.6–4 Å, coloured by domain according to panel a. d Final XPF–ERCC1 atomic model coloured by domain according to panel a, displayed within a transparent cryo-EM potential map. The XPF nuclease–(HhH)2 and ERCC1 NLD–(HhH)2 domain linker is visible at lower map thresholds. e Representative region of the cryo-EM map close to strand  ß-11 and sidechains from the final model in pink. f Representative part of the cryo-EM map close to α-helix 20 with sidechains shown from the final model in pink.

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