Crystal structure of the metazoan Nup62â¢Nup58â¢Nup54 nucleoporin complex.
Science
; 350(6256): 106-10, 2015 Oct 02.
Article
in En
| MEDLINE
| ID: mdl-26292704
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 Nup62â¢58â¢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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Nuclear Pore
/
Nuclear Pore Complex Proteins
Limits:
Animals
Language:
En
Journal:
Science
Year:
2015
Document type:
Article
Affiliation country:
Germany