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. Author manuscript; available in PMC: 2022 Apr 30.
Published in final edited form as: J Mol Biol. 2021 Mar 4;433(9):166910. doi: 10.1016/j.jmb.2021.166910

Fig. 1.

Fig. 1.

The overall structure of the XlNse1-3-4 complex.

(a) Diagram of the domain organization of XlNse1, XlNse3, and XlNse4. Nse3 residues corresponding to those mutated in the LICS patients are marked with red circles. Two Nse4 constructs used for structural analyses are marked with M and ML.

(b) 2Fo-Fc map of the Nse3 WHA-WHB linker (red line) showing the connectivity between these two domains. Thick yellow and blue lines represent Nse1 and Nse4, respectively.

(c) Ribbon representation of the structure of the Nse1 (orange)-3 (green)-4 (blue) trimeric complex. The two helices of Nse4 bind to the WHB surface of Nse3, and the extended loop threads through a channel at the interface of Nse1 and Nse3. Two zinc ions at the Nse1 RING finger domain are shown as spheres (cyan).

(d) View of the Nse1-3-4 complex rotated 180° relative to the view shown in (c).