Report

Architecture of the nuclear pore complex coat

See allHide authors and affiliations

Science  06 Mar 2015:
Vol. 347, Issue 6226, pp. 1148-1152
DOI: 10.1126/science.aaa4136

You are currently viewing the abstract.

View Full Text

Log in to view the full text

Log in through your institution

Log in through your institution

A closeup view of the nuclear pore's coat

The precise molecular architecture of the nuclear pore complex (NPC), which mediates traffic between the cytoplasm and the nucleus, has been difficult to ascertain owing to the size and complexity of this subcellular structure. Now, Stuwe et al. describe the crystal structure of the intact ç400-kD coat nucleoporin complex (CNC) of Saccharomyces cerevisiae in the presence of an engineered antibody fragment. Docking the crystal structure into an electron tomography reconstruction of the human NPC established the presence of 32 copies of the CNC arranged in four stacked rings and revealed the details of higher-order CNC oligomerization at the near-atomic level.

Science, this issue p. 1148

Abstract

The nuclear pore complex (NPC) constitutes the sole gateway for bidirectional nucleocytoplasmic transport. Despite half a century of structural characterization, the architecture of the NPC remains unknown. Here we present the crystal structure of a reconstituted ~400-kilodalton coat nucleoporin complex (CNC) from Saccharomyces cerevisiae at a 7.4 angstrom resolution. The crystal structure revealed a curved Y-shaped architecture and the molecular details of the coat nucleoporin interactions forming the central “triskelion” of the Y. A structural comparison of the yeast CNC with an electron microscopy reconstruction of its human counterpart suggested the evolutionary conservation of the elucidated architecture. Moreover, 32 copies of the CNC crystal structure docked readily into a cryoelectron tomographic reconstruction of the fully assembled human NPC, thereby accounting for ~16 megadalton of its mass.

View Full Text