5C2U

Ferredoxin-like domain of nucleoporin Nup54 bound to a nanobody

Summary for 5C2U

• Entry DOI: 10.2210/pdb5c2u/pdb
• Descriptor: Nanobody, Nup54 (3 entities in total)
• Functional Keywords: nucleoporin nup54, nup54 alpha-beta domain, ferredoxin-like fold, transport protein
• Biological source: Camelus dromedarius; More
• Total number of polymer chains: 2
• Total formula weight: 30013.40

Authors

Chug, H.,Trakhanov, S.,Hulsmann, B.B.,Pleiner, T.,Gorlich, D. (deposition date: 2015-06-16, release date: 2015-08-26, Last modification date: 2024-11-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.55 Å)