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Science. 2015 Oct 2;350(6256):106-10. doi: 10.1126/science.aac7420. Epub 2015 Aug 20.

Crystal structure of the metazoan Nup62•Nup58•Nup54 nucleoporin complex.

Author information

1
Department of Cellular Logistics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
2
Department of Cellular Logistics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany. goerlich@mpibpc.mpg.de.

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.

PMID:
26292704
DOI:
10.1126/science.aac7420
[Indexed for MEDLINE]
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