5HB4

Crystal structure of Chaetomium thermophilum Nup192

5HB4 の概要

• エントリーDOI: 10.2210/pdb5hb4/pdb
• 関連するPDBエントリー: 5HAX 5HAY 5HAZ 5HB0 5HB1 5HB2 5HB3 5HB5 5HB6 5HB7 5HB8
• 分子名称: Nup192,Nucleoporin NUP192, OSMIUM ION (2 entities in total)
• 機能のキーワード: nucleocytoplasmic transport, protein transport, transport protein
• 由来する生物種: Chaetomium thermophilum; 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 179380.42

構造登録者

Stuwe, T.,Lin, D.H.,Hoelz, A. (登録日: 2015-12-31, 公開日: 2016-04-20, 最終更新日: 2024-03-06)

主引用文献

Lin, D.H.,Stuwe, T.,Schilbach, S.,Rundlet, E.J.,Perriches, T.,Mobbs, G.,Fan, Y.,Thierbach, K.,Huber, F.M.,Collins, L.N.,Davenport, A.M.,Jeon, Y.E.,Hoelz, A.
Architecture of the symmetric core of the nuclear pore.
Science, 352:aaf1015-aaf1015, 2016

PubMed Abstract: The nuclear pore complex (NPC) controls the transport of macromolecules between the nucleus and cytoplasm, but its molecular architecture has thus far remained poorly defined. We biochemically reconstituted NPC core protomers and elucidated the underlying protein-protein interaction network. Flexible linker sequences, rather than interactions between the structured core scaffold nucleoporins, mediate the assembly of the inner ring complex and its attachment to the NPC coat. X-ray crystallographic analysis of these scaffold nucleoporins revealed the molecular details of their interactions with the flexible linker sequences and enabled construction of full-length atomic structures. By docking these structures into the cryoelectron tomographic reconstruction of the intact human NPC and validating their placement with our nucleoporin interactome, we built a composite structure of the NPC symmetric core that contains ~320,000 residues and accounts for ~56 megadaltons of the NPC's structured mass. Our approach provides a paradigm for the structure determination of similarly complex macromolecular assemblies.

PubMed: 27081075
DOI: 10.1126/science.aaf1015

実験手法

X-RAY DIFFRACTION (3.2 Å)