title: Crystal structure of the metazoan Nup62•Nup58•Nup54 nucleoporin complex.
abstract: Nuclear pore complexes (NPCs) conduct nucleocytoplasmic transport and gain transport selectivity through nucleoporin FG domains. Here, we report a structural analysis of the FG Nup62•58•54 complex, which is a crucial component of the transport system. It comprises a ≈13 nanometer-long trimerization interface with an unusual 2W3F coil, a canonical heterotrimeric coiled coil, and a kink that enforces a compact six-helix bundle. Nup54 also contains a ferredoxin-like domain. We further identified a heterotrimeric Nup93-binding module for NPC anchorage. The quaternary structure alternations in the Nup62 complex, which were previously proposed to trigger a general gating of the NPC, are incompatible with the trimer structure. We suggest that the highly elongated Nup62 complex projects barrier-forming FG repeats far into the central NPC channel, supporting a barrier that guards the entire cross section.
authors: Department of Cellular Logistics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
authors: Hema
authors: H
authors: Chug
authors: Department of Cellular Logistics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
authors: Sergei
authors: S
authors: Trakhanov
authors: Department of Cellular Logistics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
authors: Bastian B
authors: BB
authors: Hülsmann
authors: Department of Cellular Logistics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
authors: Tino
authors: T
authors: Pleiner
authors: Department of Cellular Logistics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany. goerlich@mpibpc.mpg.de.
authors: Dirk
authors: D
authors: Görlich
mesh_terms: D000818:Animals; D018360:Crystallography, X-Ray; D030562:Databases, Protein; D022022:Nuclear Pore / Q000737:chemistry / Q000648:ultrastructure*; D028861:Nuclear Pore Complex Proteins / Q000737:chemistry / Q000648:ultrastructure*; D017434:Protein Structure, Tertiary; D029867:Xenopus Proteins / Q000737:chemistry / Q000648:ultrastructure; D014982:Xenopus laevis
chemical_list: D028861:Nuclear Pore Complex Proteins; D029867:Xenopus Proteins