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Structure, Dynamics, Evolution, and Function of a Major Scaffold Component in the Nuclear Pore Complex

Authors :
Benjamin L. Timney
Andrej Sali
Zhanna Hakhverdyan
Thomas M. Weiss
Paula Upla
Stephen K. Burley
Tsutomu Matsui
Javier Fernandez-Martinez
U. Pieper
P. Sampathkumar
Jeremy Phillips
Steven C. Almo
J. Michael Sauder
David L. Stokes
Seung Joong Kim
Natalia E. Ketaren
Michael P. Rout
Jeffrey B. Bonanno
William J. Rice
Source :
Structure (London, England : 1993), vol 21, iss 4
Publisher :
Elsevier Ltd.

Abstract

Summary The nuclear pore complex, composed of proteins termed nucleoporins (Nups), is responsible for nucleocytoplasmic transport in eukaryotes. Nuclear pore complexes (NPCs) form an annular structure composed of the nuclear ring, cytoplasmic ring, a membrane ring, and two inner rings. Nup192 is a major component of the NPC's inner ring. We report the crystal structure of Saccharomyces cerevisiae Nup192 residues 2–960 [ScNup192(2–960)], which adopts an α-helical fold with three domains (i.e., D1, D2, and D3). Small angle X-ray scattering and electron microscopy (EM) studies reveal that ScNup192(2–960) could undergo long-range transition between "open" and "closed" conformations. We obtained a structural model of full-length ScNup192 based on EM, the structure of ScNup192(2–960), and homology modeling. Evolutionary analyses using the ScNup192(2–960) structure suggest that NPCs and vesicle-coating complexes are descended from a common membrane-coating ancestral complex. We show that suppression of Nup192 expression leads to compromised nuclear transport and hypothesize a role for Nup192 in modulating the permeability of the NPC central channel.

Details

Language :
English
ISSN :
09692126
Issue :
4
Database :
OpenAIRE
Journal :
Structure
Accession number :
edsair.doi.dedup.....2b2a977b54861cb00459fa05bf833d5f
Full Text :
https://doi.org/10.1016/j.str.2013.02.005