XB-ART-51475
Science
2015 Oct 02;3506256:106-10. doi: 10.1126/science.aac7420.
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Crystal structure of the metazoan Nup62•Nup58•Nup54 nucleoporin complex.
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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.
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Species referenced: Xenopus laevis
Genes referenced: nup54 nup62 nup93
References :
Ullman,
STRUCTURAL BIOLOGY. Locking down the core of the pore.
2015, Pubmed