Crystal structure of the metazoan Nup62•Nup58•Nup54 nucleoporin complex - PubMed (original) (raw)

. 2015 Oct 2;350(6256):106-10.

doi: 10.1126/science.aac7420. Epub 2015 Aug 20.

Affiliations

• PMID: 26292704
• DOI: 10.1126/science.aac7420

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

Hema Chug et al. Science. 2015.

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.

Copyright © 2015, American Association for the Advancement of Science.

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Comment in

• STRUCTURAL BIOLOGY. Locking down the core of the pore.
  Ullman KS, Powers MA. Ullman KS, et al. Science. 2015 Oct 2;350(6256):33-4. doi: 10.1126/science.aad3797. Science. 2015. PMID: 26430103 No abstract available.

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