English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Crystal structure of the metazoan Nup62•Nup58•Nup54 nucleoporin complex.

Chug, H., Trakhanov, S., Hülsmann, B. B., Pleiner, T., & Görlich, D. (2015). Crystal structure of the metazoan Nup62•Nup58•Nup54 nucleoporin complex. Science, 350(6256), 106-110. doi:10.1126/science.aac7420.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-4F55-3 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-D5BD-4
Genre: Journal Article

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Chug, H.1, Author              
Trakhanov, S.1, Author              
Hülsmann, B. B.1, Author              
Pleiner, T.1, Author              
Görlich, D.1, Author              
Affiliations:
1Department of Cellular Logistics, MPI for Biophysical Chemistry, Max Planck Society, ou_578574              

Content

show
hide
Free keywords: -
 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 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.

Details

show
hide
Language(s): eng - English
 Dates: 2015-08-202015-10-02
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1126/science.aac7420
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Science
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 350 (6256) Sequence Number: - Start / End Page: 106 - 110 Identifier: -