3T97

Molecular Architecture of the Transport Channel of the Nuclear Pore Complex: Nup62/Nup54

Summary for 3T97

• Entry DOI: 10.2210/pdb3t97/pdb
• Related: 3T98
• Descriptor: Nuclear pore complex protein Nup54, Nuclear pore glycoprotein p62 (3 entities in total)
• Functional Keywords: nucleoporin, coiled-coil, nuclear pore complex, central transport channel, alpha helical proteins, triple helix, buried polar residues, structural proteins, nucleoporins, fg repeat, nucleocytoplasmic transport, nup58, nup88, nup93, karyopherin, nuclear envelope, nuclear pore membrane domain, central channel, protein transport
• Biological source: Rattus norvegicus (rat); More
• Cellular location: Nucleus, nuclear pore complex: P70582 P17955
• Total number of polymer chains: 3
• Total formula weight: 22699.63

Authors

Chauhan, R.,Blobel, G.,Melcak, I. (deposition date: 2011-08-02, release date: 2011-11-02, Last modification date: 2024-02-28)

Primary citation

Solmaz, S.R.,Chauhan, R.,Blobel, G.,Melcak, I.
Molecular architecture of the transport channel of the nuclear pore complex.
Cell(Cambridge,Mass.), 147:590-602, 2011

PubMed Abstract: The nuclear pore complex encloses a central channel for nucleocytoplasmic transport, which is thought to consist of three nucleoporins, Nup54, Nup58, and Nup62. However, the structure and composition of the channel are elusive. We determined the crystal structures of the interacting domains between these nucleoporins and pieced together the molecular architecture of the mammalian transport channel. Located in the channel midplane is a flexible Nup54⋅Nup58 ring that can undergo large rearrangements yielding diameter changes from ∼20 to ∼40 nm. Nup62⋅Nup54 triple helices project alternately up and down from either side of the midplane ring and form nucleoplasmic and cytoplasmic entries. The channel consists of as many as 224 copies of the three nucleoporins, amounting to a molar mass of 12.3 MDa and contributing 256 phenylalanine-glycine repeat regions. We propose that the occupancy of these repeat regions with transport receptors modulates ring diameter and transport activity.

PubMed: 22036567
DOI: 10.1016/j.cell.2011.09.034

Experimental method

X-RAY DIFFRACTION (2.8 Å)