2QX5

Structure of nucleoporin Nic96

2QX5 の概要

• エントリーDOI: 10.2210/pdb2qx5/pdb
• 分子名称: Nucleoporin NIC96, CHLORIDE ION (3 entities in total)
• 機能のキーワード: nucleoporin, mrna transport, nuclear pore complex, nucleus, protein transport, translocation, transport, transport protein
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Nucleus, nuclear pore complex: P34077
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 151829.70

構造登録者

Jeudy, S.,Schwartz, T.U. (登録日: 2007-08-10, 公開日: 2007-09-25, 最終更新日: 2024-02-21)

主引用文献

Jeudy, S.,Schwartz, T.U.
Crystal structure of nucleoporin Nic96 reveals a novel, intricate helical domain architecture
J.Biol.Chem., 282:34904-, 2007

PubMed Abstract: The nuclear pore complex (NPC) is an elaborate protein machine that mediates macromolecular transport across the nuclear envelope in all eukaryotes. The NPC is formed by nucleoporins that assemble in multiple copies around an 8-fold symmetry axis. Homology modeling suggests that most architectural nucleoporins are composed of simple beta-propeller and alpha-helical repeat domains. Here we present the crystal structure of Nic96, the Nup93 homolog in Saccharomyces cerevisiae, one of the major components of the NPC. This is the first structure of an alpha-helical nucleoporin domain. The protein folds into an elongated, mostly alpha-helical structure. Characteristically, non-canonical architectural features define the Nic96 structure. Sequence conservation among Nup93 homologs across all eukaryotes strongly suggests that the distinct topology is evolutionarily well maintained. We propose that the unique Nic96/Nup93 fold has a conserved function in all eukaryotes.

PubMed: 17897938
DOI: 10.1074/jbc.M705479200

実験手法

X-RAY DIFFRACTION (2.5 Å)