5C3L

Structure of the metazoan Nup62.Nup58.Nup54 nucleoporin complex.

5C3L の概要

• エントリーDOI: 10.2210/pdb5c3l/pdb
• 分子名称: Nup54, Nucleoporin Nup58, Nucleoporin Nup62, ... (5 entities in total)
• 機能のキーワード: nucleoporin, heterotrimeric coiled coils, kink containing coiled-coils, six helix-bundle, transport protein
• 由来する生物種: Xenopus laevis (African clawed frog); 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 84695.56

構造登録者

Chug, H.,Trakhanov, S.,Hulsmann, B.B.,Pleiner, T.,Gorlich, D. (登録日: 2015-06-17, 公開日: 2015-08-26, 最終更新日: 2024-11-20)

主引用文献

Chug, H.,Trakhanov, S.,Hulsmann, B.B.,Pleiner, T.,Gorlich, D.
Crystal structure of the metazoan Nup62Nup58Nup54 nucleoporin complex.
Science, 350:106-110, 2015

PubMed 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.

PubMed: 26292704
DOI: 10.1126/science.aac7420

実験手法

X-RAY DIFFRACTION (2.9 Å)