5C3L
Structure of the metazoan Nup62.Nup58.Nup54 nucleoporin complex.
Summary for 5C3L
| Entry DOI | 10.2210/pdb5c3l/pdb |
| Descriptor | Nup54, Nucleoporin Nup58, Nucleoporin Nup62, ... (5 entities in total) |
| Functional Keywords | nucleoporin, heterotrimeric coiled coils, kink containing coiled-coils, six helix-bundle, transport protein |
| Biological source | Xenopus laevis (African clawed frog) More |
| Total number of polymer chains | 5 |
| Total formula weight | 84695.56 |
| Authors | Chug, H.,Trakhanov, S.,Hulsmann, B.B.,Pleiner, T.,Gorlich, D. (deposition date: 2015-06-17, 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 Cited by 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: 26292704DOI: 10.1126/science.aac7420 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
Download full validation report
