5c3l
Structure of the metazoan Nup62.Nup58.Nup54 nucleoporin complex.Structure of the metazoan Nup62.Nup58.Nup54 nucleoporin complex.
Structural highlights
FunctionPublication Abstract from PubMedNuclear 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 approximately 13 nm 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 NPC-gating, 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. Crystal structure of the metazoan Nup62*Nup58*Nup54 nucleoporin complex.,Chug H, Trakhanov S, Hulsmann BB, Pleiner T, Gorlich D Science. 2015 Aug 20. pii: aac7420. PMID:26292704[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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