Fontanaet al., Science 376 , eabm9326 (2022) 10 June 2022 7of11
Fig. 4. Nup358 interacts with the Y-complexes as clamps.(A) Domain
organization ofX. laevisNup358 and the approximate boundaries. ZnFs, zinc
fingers. (B) AlphaFold-predicted structure of the N-terminal region of Nup358,
showing the S-shaped globular domain, an isolated helix, and the flexible
linker in between. (C) Fitting of Nup358 globular domain to the density (contour
level, 8.0s). ( D) The region of the map (contour level, 8.0s) containing five
Nup358 molecules (labeled as clamps A to E) and two Y-complexes (Nup96-
Nup107 complex), in two orientations. (E) Two Nup358 molecules each clamp
around Nup96-Nup107 at the inner and outer Y-complexes. Clamps A and B
(red) are for the outer Y-complex, and clamps C and D (pink) are for the
inner Y-complex. The last Nup358 (clamp E, orange) contacts clamp C and
Nup107 of the outer Y-complex. (F) Relative shifts in the clamp location on
the two Y-complexes. The clamps B and D are similar in their location on Nup107,
whereas clamps A and C have a shift in their position on Nup96.RESEARCH | STRUCTURE OF THE NUCLEAR PORE