4XMM

Structure of the yeast coat nucleoporin complex, space group C2

Summary for 4XMM

• Entry DOI: 10.2210/pdb4xmm/pdb
• Related: 4XMN
• Descriptor: Protein transport protein SEC13, Nucleoporin NUP145, Nucleoporin SEH1, ... (8 entities in total)
• Functional Keywords: structural protein, immune system, transport protein-immune system complex, transport protein/immune system
• Biological source: Saccharomyces cerevisiae S288c (Baker's yeast); More
• Total number of polymer chains: 8
• Total formula weight: 454644.03

Authors

Stuwe, T.,Correia, A.R.,Lin, D.H.,Paduch, M.,Lu, V.T.,Kossiakoff, A.A.,Hoelz, A. (deposition date: 2015-01-14, release date: 2015-03-25, Last modification date: 2024-11-20)

Primary citation

Stuwe, T.,Correia, A.R.,Lin, D.H.,Paduch, M.,Lu, V.T.,Kossiakoff, A.A.,Hoelz, A.
Nuclear pores. Architecture of the nuclear pore complex coat.
Science, 347:1148-1152, 2015

PubMed 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.

PubMed: 25745173
DOI: 10.1126/science.aaa4136

Experimental method

X-RAY DIFFRACTION (7.384 Å)