3T98
Molecular Architecture of the Transport Channel of the Nuclear Pore Complex: Nup54/Nup58
Summary for 3T98
Entry DOI | 10.2210/pdb3t98/pdb |
Related | 2OSZ 3T97 |
Descriptor | Nuclear pore complex protein Nup54, Nucleoporin Nup58/Nup45 (3 entities in total) |
Functional Keywords | nup58, nup54, nup62 complex, nuclear import, coiled-coil, helix, hairpin, fg-repeat, nucleoporin, npc, nuclear tranport, transport channel, nup62, nup45, nup93, karyopherin, nuclear pore complex, nuclear pore domain, nuclear envelope, protein transport |
Biological source | Rattus norvegicus (rat) More |
Cellular location | Nucleus, nuclear pore complex: P70582 P70581 |
Total number of polymer chains | 3 |
Total formula weight | 22788.94 |
Authors | Solmaz, S.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 Cited by 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: 22036567DOI: 10.1016/j.cell.2011.09.034 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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