2OSZ

Structure of Nup58/45 suggests flexible nuclear pore diameter by intermolecular sliding

Summary for 2OSZ

• Entry DOI: 10.2210/pdb2osz/pdb
• Descriptor: Nucleoporin p58/p45 (2 entities in total)
• Functional Keywords: npc, nucleoporin, structural protein
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Nucleus, nuclear pore complex : P70581
• Total number of polymer chains: 4
• Total formula weight: 43124.76

Authors

Melcak, I.,Hoelz, A.,Blobel, G. (deposition date: 2007-02-06, release date: 2007-04-10, Last modification date: 2024-02-21)

Primary citation

Melcak, I.,Hoelz, A.,Blobel, G.
Structure of Nup58/45 suggests flexible nuclear pore diameter by intermolecular sliding.
Science, 315:1729-1732, 2007

PubMed Abstract: The nucleoporins Nup58 and Nup45 are part of the central transport channel of the nuclear pore complex, which is thought to have a flexible diameter. In the crystal structure of an alpha-helical region of mammalian Nup58/45, we identified distinct tetramers, each consisting of two antiparallel hairpin dimers. The intradimeric interface is hydrophobic, whereas dimer-dimer association occurs through large hydrophilic residues. These residues are laterally displaced in various tetramer conformations, which suggests an intermolecular sliding by 11 angstroms. We propose that circumferential sliding plays a role in adjusting the diameter of the central transport channel.

PubMed: 17379812
DOI: 10.1126/science.1135730

Experimental method

X-RAY DIFFRACTION (2.85 Å)