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4XMN

Structure of the yeast coat nucleoporin complex, space group P212121

Summary for 4XMN
Entry DOI10.2210/pdb4xmn/pdb
Related4XMM
DescriptorProtein transport protein SEC13, Nucleoporin NUP145, Nucleoporin NUP84, ... (7 entities in total)
Functional Keywordsstructural protein, protein transport
Biological sourceSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
More
Cellular locationCytoplasmic vesicle, COPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side: Q04491
Nucleoporin NUP145C: Nucleus, nuclear pore complex. Nucleoporin NUP145N: Nucleus, nuclear pore complex: P49687
Nucleus, nuclear pore complex: P52891 P35729 P46673
Total number of polymer chains7
Total formula weight413525.01
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: 2024-11-06)
Primary citationStuwe, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (7.6 Å)
Structure validation

237735

数据于2025-06-18公开中

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