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Assembly of Nsp1 Nucleoporins Provides Insight into Nuclear Pore Complex Gating

Figure 1

Initial and final configuration of simulated wild-type Nsp1-FGs grafted to a gold ring (simulation wild-type_ring).

(a) Initial configuration. Shown are fully-extended, wild-type Nsp1-FGs grafted on the ring, the geometry of which matches that of an experimentally constructed nanodevice mimicking an NPC as reported in [21], [29]. Colors distinguish 120 wild-type Nsp1-FGs grafted on the ring in three concentric rows. (b) Close-up view of grafted ends of the Nsp1-FG chains. The gold nano-ring is cut open to expose the C-termini, shown as red spheres, fixed to the gold ring, as well as the terminal parts of the Nsp1-FG chains. (c) Snapshot of the () end of simulation wild-type_ring. One can recognize that the Nsp1-FG chains, shown in surface representation, have formed brush-like bundles. (d) Close-up view of the structure in (a). Shown is a region as marked. The close-up view reveals the initially straight conformation of the Nsp1-FG chains; bumps in the surface of the individual chains correspond to amino acid side groups. (e) Close-up view of a segment of (c). The view reveals the brush-like bundles formed by the Nsp1-FG chains. Arrows point to cross-links between bundles formed when single Nsp1-FG chains cross from one bundle to another bundle. As a result of such cross-links the bundles form a mesh of thick (bundles made of several Nsp1-FG chains) and thin (cross-links made of single Nsp1-FG chains) segments. Video S1 shows how during simulation wild-type_ring the initially completely extended Nsp1-FG chains assume random conformations and form bundles as those seen here. Video S2 provides a three-dimensional view, reached through rotating the system in front of the viewer, of the conformation reached in simulation wild-type_ring after , namely the conformation depicted in (c) and (e).

Figure 1

doi: https://doi.org/10.1371/journal.pcbi.1003488.g001