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Assembly of Nsp1 Nucleoporins Provides Insight into Nuclear Pore Complex Gating

Figure 3

Initial and final configuration of a simulated array of wild-type Nsp1-FGs grafted to a gold substrate (simulation random_array).

(a) Initial configuration. Shown is the 5×5 array of wild-type Nsp1-FGs grafted with their C-terminal ends to a gold substrate. The proteins are placed initially in random polymer-like conformations obtained computationally through a description of non-overlapping worm-like chains. Colors distinguish the 25 grafted wild-type Nsp1-FGs. (b) Close-up view of grafted ends of the Nsp1-FG chains in an array. Shown as red spheres are C-terminal ends of the Nsp1-FG chains fixed to the gold substrate, as well as the terminal segments of the Nsp1-FG chains. (c) Snapshot of the () end of simulation random_array. One can see that the end-tethered, randomly placed (matching a worm-like chain model) Nsp1-FGs, shown in surface representation, form brush-like structures as in case of simulation wild-type_ring, but with a higher density of cross-links compared to the gold ring case shown in Figure 1. (d) Close-up view of a segment of (c). The view reveals cross-linked Nsp1-FG bundles. Arrows point to cross-links between bundles formed when Nsp1-FG chains cross from one bundle to another bundle. Video S3 shows how during simulation random_array the initially completely random conformation of Nsp1-FG chains assume a mesh-like structure by cross-linking between thin bundles as those seen here. Video S4 provides a 360-degree view of the conformation reached in simulation random_array after , namely the conformation depicted in (c) and (d).

doi: https://doi.org/10.1371/journal.pcbi.1003488.g003