2Q5Y

Crystal Structure of the C-terminal domain of hNup98

2Q5Y の概要

• エントリーDOI: 10.2210/pdb2q5y/pdb
• 分子名称: Nuclear pore complex protein Nup98, Nuclear pore complex protein Nup96 (3 entities in total)
• 機能のキーワード: nup98, nucleoporin, autoproteolysis, protein transport
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus membrane ; Peripheral membrane protein; Nucleoplasmic side : P52948 P52948
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 36030.78

構造登録者

Sun, Y.,Guo, H.C. (登録日: 2007-06-03, 公開日: 2008-10-14, 最終更新日: 2024-02-21)

主引用文献

Sun, Y.,Guo, H.C.
Structural constraints on autoprocessing of the human nucleoporin Nup98.
Protein Sci., 17:494-505, 2008

PubMed Abstract: Nucleoporin Nup98, a 98-kDa protein component of the nuclear pore complex, plays an important role in both protein and RNA transport. During its maturation process, Nup98 undergoes post-translational autoproteolysis, which is critical for targeting to the NPC. Here we present high-resolution crystal structures of the C-terminal autoproteolytic domains of Nup98 (2.3 A for the wild type and 1.9 A for the S864A precursor), and propose a detailed autoproteolysis mechanism through an N-O acyl shift. Structural constraints are found at the autocleavage site, and could thus provide a driving force for autocleavage at the scissile peptide bond. Such structural constraints appear to be generated, at least in part, by anchoring a conserved phenylalanine side chain into a highly conserved hydrophobic pocket at the catalytic site. Our high-resolution crystal structures also reveal that three highly conserved residues, Tyr866, Gly867, and Leu868, provide most of the interactions between the autoproteolytic domain and the C-terminal tail. These results suggest that Nup98 may represent a new subtype of protein that utilizes autoprocessing to control biogenesis pathways and intracellular translocation.

PubMed: 18287282
DOI: 10.1110/ps.073311808

実験手法

X-RAY DIFFRACTION (2.3 Å)